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Istilah SEMUT JEPANG sudah banyak digunakan oleh masyarakat, tapi sebenarnya tidak mencirikan sebagai semut.
Lebih cocok disebut kutu beras Tenebrio Molitor.
Perbedaan dari semut Jepang dibandingkan semut spesies lainnya yakni memiliki badan yang keras, bersayap
namun tak bisa terbang, suka reproduksi, hidup secara berkelompok, bukan hewan kanibal.
Sumber :

BBPPTP Ambon, Ulat tepung (Tenebrio molitor) dikenal juga oleh

kebanyakan masyarakat sebagai ulat hongkong. Imago dari serangga ini
berupa kumbang yang termasuk dalam genusTenebrio yang memiliki warna
merah kehitaman, hitam atau coklat gelap dan panjangnya 13-17 mm
(Borror et al., 1982).
Sumber :

Ciri dari semut jepang ini secara umum adalah memiliki tubuh berwarna hitam kecoklatan, berkaki enam dan tekstur
tubuhnya cenderung keras. Hewan ini memiliki sayap yang mirip dengan kumbang. Namun semut jepang tidak dapat
terbang seperti serangga bersayap lainya.

Sumber :
Keunikan khas Semut jepang
Semut jepang memiliki ciri atau tanda seperti:
Suka atau cepat berkembangbiak

Hidup berkoloni atau berkelompok


Ruas badan lebih besar dari ruas kepala


Ukuran tubuh kecil hanya beberapa milimeter


Bukan tipe hewan pemakan daging/sesama


Memiliki sayap tapi tidak bisa terbang


Makanan ragi tape


Memiliki badan yang keras,


Memiliki kaki 6

Sumber :
Manfaat dan kegunaan dari semut Jepang menurut, adalah :

Semut Jepang berguna untuk menjadikan tingkat kolesterol di darah normal, khususnya untuk orang yang
mempunyai kadar kolesterol tinggi pada darah.

Mengobati dan meringankan penyakit jantung.

Mengobati dan meringankan penyakit asam urat, khusus orang dengan kadar asam urat tinggi di tubuh.

Menjadikan jumlah gula di darah menjadi stabil, cocok untuk orang yang terserang penyakit diabetes.

Menjadikan tekanan darah stabil, khususnya untuk orang yang menderita hipertensi (penyakit darah tinggi).

Mampu menambah vitalitas dari pria maupun wanita, cocok bagi pria maupun wanita dengan jam kerja
tinggi serta kesibukan untuk sehari-harinya, tubuh pun dapat menjadi lebih segar dengan semut Jepang.

Manfaat semut Jepang berdasarkan kajian ilmiah, kami

paparkan sebagai berikut :


Sumber :

Hasilnya penelitian menunjukkan bahwa fungsi Tenebrio molitor pada tikus adalah dapat meningkatkan
pertumbuhan, meningkatkan kemampuan belajar dan menghafal serta merupakan anti kelelahan dan kekurangan
oksigen dan meningkatkan intelegent.

Sumber :
Hasilnya penelitian menunjukkan bahwa Tenebrio molitor merupakan protein alami berkualitas tinggi, namun
penggunaannya baru sebatas hal yang terkait dengan kesehatan - karena keterbatasan teknologi.

Sumber :

Sumber :



Characteristics of Maize Flour Tortilla Supplemented

with Ground Tenebrio molitorLarvae
Erick D. Aguilar-Miranda , Mercedes G. Lpez , Clara Escamilla-Santana , and Ana P. Barba de la Rosa *
Instituto Tecnolgico de Celaya, Avenida Tecnolgico s/n, Celaya, Guanajuato 38010, Mxico; Departamento de
Biotecnologa y Bioqumica, CINVESTAV-IPN, Km. 9.6 Libramiento Norte Carretera Irapuato-Len, Irapuato,
Guanajuato 36500, Mexico; and CES Internacional and Asociados, Cirilo Conejo 6, Quertaro, Quertaro, Mxico
The larva of the Tenebrio molitor, known as the yellow meal worm, is a plague of wheat and flours. Consumption of
the raw insects is not well accepted because of their appearance. The objective of the present work was to grow T.
molitor larvae under standard conditions, to analyze the chemical composition of the larvae powder, and to prepare
supplemented maize tortillas. Protein and fat contents were performed with standard methods. Tenebrio larvae
powder had a 58.4% protein content; this protein was rich in essential amino acids such as phenylalanine, tyrosine,
and tryptophan; the found values satisfied those recommended by the Food and Agriculture Organization. Fatty acid
composition was determined by GC-MS showing high contents of oleic acid and linoleic acid (19.8 and 8.51%,
respectively). A large proportion of unsaturated fatty acids of longer chains was detected. Long-chain fatty acids
having two or three double bonds have been claimed as highly beneficial to health. Tortillas supplemented
with larvae powder had excellent consumer acceptance, and tortilla protein content increased by 2% as well
as the amount of essential amino acids. These results show new ways to consume insects and at the same time
increase the nutritional value of the original food products.

--------------------------------------------------------------------------Energy-efficient food production to reduce global

warming and ecodegradation: The use of edible
Shri Manakula Vinayagar College of Engineering and Technology, Puducherry, India.

As the global population continues to rise, and attempts to increase arable land area come in sharp conflict with the
necessity to retain forests on one hand and pressures of urbanization on the other, the wave of global food shortage
that has hit the world recently is likely to hit us again and again.
The increasing pressure on land is making meat production from macro-livestock less sustainable than ever before.
To add to the diminishing pastures and broadening demand-supply gap of food grains are the shortages arising due
to the diversion of some of the food crops for biofuel production. There is also an increasing use of fodder for
generating biomass energy. The result is that even as the demand for animal protein keeps on rising with the swelling
global population, there is every possibility that attempts to meet this demand would face serious crises in the coming
years. The adverse impacts of global warming are conspiring to make the situation even worse than it otherwise
would have been.
The present review brings home the fact that one of the possible ways to get around this problem is to extend the
practice of entomophagy use of insects as human food. As of now entomophagy is practiced in some regions and
some cultures, but, by-and-large, the bulk of global population stay away from it. It is even looked down in several
cultures and forbidden in some others. The review brings out the irrationality of omitting edible insects from
human diet given the generally higher quality of nutrition they contain as compared to food based on macro-livestock.
This aspect, coupled with much lesser consumption of energy and natural resources associated with insect-based
protein production, makes entomophagy an option which deserves urgent global attention.
The authors highlight the relatively stronger sustainability of animal protein production by way of insect farming
because, pound to pound, the production of insect protein takes much less land and energy than the more widely

consumed forms of animal protein. It is estimated that over a thousand insect species are already a part of human
diet and the nutrition offered by several of the species matches or surpasses that which is contained in traditional
non-vegetarian foods. The paper also deals with the relevance of entomophagy as a potentially more ecologically
compatible and sustainable source of animal protein than the red and the white meat on which most of the world
presently depends. In the emerging global pattern based on an expanding share of renewable energy sources,
entomophagy fits in as a renewable source of food energy for the future.

----------------------------------------------------------Larvae of mealworm (Tenebrio molitor L.) as European

novel food
Copyright 2013 Ewa Siemianowska et al. This is an open access article distributed under the Creative Commons
Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the
original work is properly cited.

For centuries, insects have been used as food due to their availability and easiness in raising
that is much lessburdensome for environment than animal husbandry breeding. Mealworm
(Tenebrio molitor L.)
larvae are consumed by
people. The aim of the work was to determine the nutritional value of
molitor L.).
material was a three-month-old mealworm larva
25 - 30 mm in length. Larvaewere boiled for 3 min and next dried in 60C. Contents of water, ash
been determined. Fresh larvae contained 56% of water, 18% of total protein, 22% of total fat and
1.55% of ash.High contents of minerals were found in the larvae: magnesium (87.5 mg/100g),
zinc (4.2 mg/100g), iron (3.8 mg/100g), copper (0.78 mg/100g) and manganese (0.44 mg/100g).
The proportion of n-6/n-3 fatty
acids was very
advantageous and amounted
to 6.76. Larvae
powder contained twice higher content of protein, fat, ash and minerals. Larva of mealworm is
a valuable source of nutrients in amounts more profitable for human organism than traditional
meat food. Powdered larva is a high-grade product to be applied as a supplement to traditional

---------------------------------------------------------A digestive prolyl carboxypeptidase in Tenebrio molit

or larvae
Irina A. Goptar a, Dmitry A. Shagin b, c, Irina A. Shagina c, Elena S. Mudrik c, Yulia A. Smirnova d, Dmitry
P. Zhuzhikov e,Mikhail A. Belozersky d, Yakov E. Dunaevsky d, Brenda Oppert f, *, Irina Yu. Filippova a, El
ena N. Elpidina d
a Chemical Faculty, Moscow State University, Moscow 119991, Russia
b Shemiakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, Miklukho-Maklaya 16/10, 117997 Moscow, Russia
c Evrogen JSC, Miklukho-Maklaya 16/10, 117997 Moscow, Russia
d A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russia
e Biological Faculty, Moscow State University, Moscow 119991, Russia
f USDA Agricultural Research Service, Center for Grain and Animal Health Research, 1515 College Ave., Manhattan, KS 66502, USA

Prolyl carboxypeptidase (PRCP) is a lysosomal proline specic serine peptidase that also
plays a vital role

in the regulation of physiological processes in mammals. In this report, we

isolate and characterize the
rstPRCP in an insect. PRCP was puried from the anterior midgut of larvae of a stored prod
uct pest, Tenebrio molitor, using a three-step chromatography strategy, and it was determined
that the puried
enzyme was a dimer. The cDNA of PRCP was cloned and sequenced, and the predicted pro
tein was
identical to theproteomic sequences of the puried enzyme. The substrate specicity and kinet
ic parameters of the enzymewere determined. The T. molitor PRCP participates in the hydrol
ysis of
the insects major dietary proteins,gliadins, and is
the rst PRCP
to be ascribed a digestive function. Our
collective data suggest that theevolutionary enrichment of the digestive peptidase complex in i
with an area of acidic to
neutral pH inthe
midgut is a result of the incorporation of lysosomal peptidases, including PRCP.
Prolyl carboxypeptidase (PRCP; PCP, lysosomal carboxypeptidase,
angiotensinase C, EC belongs to agroup of proline specic
peptidases (PSP) (Cunningham and OConnor, 1997) that are involved in the regulationof variou
metabolic processes (Vanhoof et al., 1995). PSP represent a relatively small group of highly sp
ecicexo- and
endo-peptidases that cleave
bonds formed by proline residues in
proteins and peptides. The unique
activity of PSP is due to the
structural features of proline, the only cyclic imino acid among 20 amino acidsfound in prote
ins and peptides. Peptide bonds containing
proline residues are not hydrolyzed efciently by mostpeptidases,
and a proline residue in the peptide chain serves to protect against
degradation by enzymes withbroad specicity. The ability of PSP to hydrolyze this bond determ
ines the specic activity of the enzyme in theregulation of metabolic processes.
PRCP are serine peptidases that catalyze the
cleavage of a substrate
at the Cterminal amino acid
linked to aproline residue. At present,
only PRCP from human (Odya et al., 1978; Tan et al., 1993; Shariat- Madar et al.,2002), pig (
Yang et al., 1970; Kakimoto et al., 1973), monkey (Suzawa et al., 1995), and bacteriumXanth
omonas malto- philia (Suga et al., 1995) have been isolated and studied. The primary
structure of theisolated enzyme, present as a dimer in solution, has
been described only for human PRCP, and the enzyme wasassigned to
the S28 family of
serine peptidases (Tan et al., 1993). The crystal
structure was solved recentlyand revealed that PRCP has a unique
peptidase structure, with closest identity to dipeptidyl peptidase 7
(DPP7), containing a conserved a/b hydrolase domain and a novel
helical SKS domain that caps the active site with thecatalytic Ser-Asp- His triad (Abeywickrema
et al., 2010; Soisson et al., 2010).
PRCP is widely distributed in human tissues, but mostly it is localized to the lungs, liver
and placenta(Tan et al., 1993). The enzyme was initially found in human lysosomes (Yang et
al., 1970; Kumamoto et al.,1981), but later it was found as a membrane- expressed enzyme in
cultured human umbilical vein endothelial

cells, explained by the association of PRCP with specic membrane

proteins after exocytosis (Shariat-Madar etal., 2004).
The exact physiological
functions for PRCP are not completely
understood. The key role
for mammalian PRCP is in regulating
blood pressure (Kumamoto et al., 1981; Tamaoki et al., 1994; Kaplan andGhebrehiwet, 2010; Ha
gedorn, 2011), but PRCP is also involved
in processes
proliferation (Duan et al., 2011), inammation (Kumamoto et al., 1981; Ngo et al., 2009) and a
ngiogenesis (Mallela et al., 2009). PRCPalso regulates food
intake by inactivating amelanocyte stimulating hormone (Wallingford et al., 2009;Shariat- Madar et al., 2010; Diano,
2011; Jeong et al., 2012). The only report
of insect PRCP details changesin expression of the PRCP gene in
response to magnesium exposure in Culex quinquefasciatus larvae (Zhao et al., 2010).
The present research on insect PSP is a part of our studies
digestive enzymes in larvae of the yellow mealworm, Tenebrio
molitor (Coleoptera: Tenebrionidae), a pest of processed grains and
storedproducts. The complex of digestive peptidases in T.
substantially from human digestive
although both the beetle and people
have grain products as a pri- mary food source. The major digestive organ of the larvae is the
midgut, where a sharp pH gradient is found, from 5.6 in the anterior
midgut (AM) to 7.9 in posterior midgut (PM) (Terra et al., 1985; Vinokurov et al., 2006a; El
pidina andGoptar, 2007). This gradient
the activity of different digestive enzymes in specic
compartmentsof the midgut, which is usually consistent with the
pHoptima of their activity (Vinokurov et al., 2006b).
The major
digestive peptidases in the AM of T. molitor larvae are
cysteine peptidases, represented
by four to six distinct enzymes
(Terra and Cristofoletti, 1996; Vinokurov et al., 2006a,b; Prabhakar et al., 2007). The major cys
teine peptidase activity
is cathepsin L
(Cristofoletti et al., 2005; Beton et al., 2012; Oppert et al.,2012) known as a lysosomal peptida
se in eukaryotes (Turk et al., 2012). In the PM of T. molitor larvae,digestive enzymes are m
ostly serine
peptidases, including four trypsin-like
and ve chymotrypsin-like
(Tsybina et al., 2005; Elpidina et al., 2005; Vinokurov et al., 2006a,b) as well as amembr
ane-bound aminopeptidase (Cristofoletti
and Terra, 1999, 2000) and soluble carboxypeptidase(Ferreira et al., 1990; Prabhakar et al., 20
The major dietary proteins of T. molitor larvae, prolamins, contain 30-50% glutamine
and 10-30%proline residues (Shewry and Tatham, 1990; Shewry and Halford, 2002).
Therefore, we analyzed the major post-glutamine cleaving activities in the T.
molitor larval digestive
complex and found that they were
cysteine peptidases (Goptar et al., 2012). Based on the composition
of their diet, we also predicted theoccurrence of digestive PSP in T. molitor larvae. Indeed,
described the rst proline-specic
digestivepeptidase in the midgut, which was a serine peptidase
that specically cleaved after proline, had an acidicpH optimum
(5.3), and was found mainly in the AM contents (Goptar et al., 2008a,b), but the enzyme w

asnot identied. In the present study,

we identify this enzyme as a PRCP and detail the substrate specicity andkinetic parameters of the rst puried PRCP in an insect.
Our data suggest that PRCP is a digestive enzyme inT.
which is a novel function for PRCP.

molitor larvae,

In this paper, the rst PRCP was isolated from an insect, T.
larvae. For PRCP
purication, a three-stage scheme was used. The
rst stage was by gel ltration. The application of
this type of
chromatographyeffectively separated PRCP, with a molecular mass
of 105 kDa, from the major digestive serine and cysteineendopeptidases, with molecular masses less than 40 kDa (Vinokurov et al., 2006b) and therefore
prevented proteolysis by
endopeptidases during purication. Additional purication followed with
anionexchange and hydrophobic chromatography, resulting in
relatively pure enzyme. The cDNA of the T. molitorlarval PRCP was
cloned and sequenced,
and the identity of
the predicted PRCP
sequence to the primary
structure of the isolated enzyme was
conrmed by mass spectrometry. The ratio of the calculated molecularmass of cloned PRC
P and that determined by gel ltration
suggests that the enzyme is a dimer, and similardata are reported
for the human lysosomal PRCP (Odya et
al., 1978; Tan et al., 1993). Also similar to thehuman PRCP, T. molitor PRCP displays acidi
c pH
optimum at pH 5.6, correlating with its localization in theacidic AM
of T. molitor larvae (Goptar et al., 2008b).
Previously, the primary structure of the enzyme was solved only
for human PRCP, and the enzyme wasassigned to the S28 family of
serine peptidases (Tan et al., 1993). When PRCP was compared with
annotatedsequences of
serine carboxypeptidases
and POP, there was a low degree of
overall identity (10e18%), but a high (67%) identity in active site amino acid residues. The
authors concluded
that PRCP is an evolutionarylink connecting two families, POP and
serine carboxypeptidases,
because they possess properties characteristic
of both families. Like serine carboxypeptidases, PRCP
catalyzes the hydrolysis of a Cterminalresidue that has
a free
carboxyl group at acidic pH values. On the other hand,
PRCP hydrolyzes bondsformed by the carbonyl group of proline residues as
do POP, and a specic inhibitor of POP, Z-Pro-prolinal,inactivates PRCP as well.
Resolution of the 2.8 A crystal structure of the human lysosomal
PRCP (Soisson et al., 2010) delineated thestructural basis of the
different substrate specicities of the two enzymes comprising the
unique S28
family ofPSP: carboxypeptidase PRCP and aminopeptidase DPP7.
PRCP has an extended active-site
cleft that can
accommodate proline substrates with multiple N-terminal
residues. In contrast, the substrate bindinggroove of DPP7 is occluded
by a short amino acid
insertion unique to DPP7 that creates a
site selective for dipeptidyl proteolysis of N-ter- minal substrates.

The most specic substrate for T. molitor PRCP was N-protected

peptide ZPF, a selective substrate for PRCP, but the activity assay
with this substrate was rather
Because serine
carboxypeptidases,unlike metallocarboxypeptidases, are
able to hydrolyze chromogenic p-nitroanilide substrates with adetectable
rate (Scheer et al., 2011), and due to the simplicity of the assay
method, we used these substratesfor
monitoring of the purication process and for the study of the substrate specicity. The best
peptide substrate was Z-AAP-pNA with the highest
Vmax/Km value, despite the fact that the substrate
hadthe lowest Km value. The hydrolysis of substrates Z-AP-pNA and AP-pNA occurred
equal efciency, although Z-AP-pNA was more
tightly bound to the enzyme, and AP-pNA was hydrolyzedfaster. Lengthening or shortening
the substrate by
one Ala residue,
substituting Ala at Gly, as well asremoving the Nprotecting group all led to an increase of the Km. The maximum rate of hydrolysis of Z-GPpNA, a specic substrate for POP (Cunningham and OConnor, 1997) and Z-P-pNA
was an orderof magnitude lower than for the other substrates.
Kinetic studies revealed complete competitive inhibition of T. molitor PRCP by Z-Proprolinal. In thistype of inhibition, the inhibitor interacts with the same region of
the enzyme that binds
substrate. Thereforethe inhibitor competes with the substrate for
interaction with the enzyme, as do other substrate-like inhibitors similar to Z-Pro-prolinal.
In contrast to human PRCP, which specically functions as a regulatory enzyme affecting
the bloodsystem (Hagedorn,
2011; Adams et al., 2011), the PRCP from T. molitor is presumably a
digestiveenzyme. Earlier, we described the localization and functions of two PSPs from T. molitor larvae (Goptar et al.,2008a,b). We demonstrated that one of th
e PSPs had an acidic pH optimum, was
localized in the AM
contents,and the activity prole changed in the
digestive process similar to the general proteolytic activity, but thesedata were insufcient
for conclusive identication of this
peptidase. In
this report, we identied thisenzyme as PRCP and
further demonstrate that T. molitor
larval PRCP participates in gliadin hydrolysis thatis reduced by a specic inhibitor of PRCP
Z- Pro-prolinal.
Thus, we
have isolated, puried, and identied the primary
structure and further characterized a digestivePRCP from the larval
midgut of
an insect pest, T. molitor. The unique aspects of this
enzyme are that it isthe rst PRCP isolated
from an insect, and the
rst PRCP found to function as
a secreted digestive enzyme. Itis
unknown if PRCP is involved in digestion in other animals. Specic
digestive peptidases in insects thatdifferentiate the mode of gliadin hydrolysis from that of hum
an include cysteine peptidases with
cleaving activity (Goptar et al., 2012), and PRCP
with postproline cleaving activity (this report).In eukaryotic organisms, these enzymes participate in the
intracellular lysosomal
degradation of proteins.Many insects rely on typical serine digestive peptidases, trypsin and c
hymotrypsin, but some groups of insectswith an area of acidic to neutral pH in the midgut use
cathepsins also for
digestion (Terra andFerreira, 1994). Our data

suggest that the enrichment of the peptidase digestive complex in

such insects duringevolution is due to the adaptation of peptidases
present in the lysosomes of eukaryotic organisms, such ascysteine cathepsins and PRCP.





Carboxypeptidase sikat enzim perbatasan pankreas yang membagi satu asam amino pada suatu waktu.

--------------------------------------------------------Supplementation of L-carnitine in athletes:

does it make sense?
Heidrun Karlic, PhD, and Alfred Lohninger, PhD
From the Ludwig Boltzmann Institute for Leukemia Research and Hematology, Vienna,
Austria; andthe Department of Medical Chemistry, University of Vienna, Vienna, Austria

Studies in athletes have shown that carnitine supplementation may foster exercise performance.
As reported in the majority of studies, an increase in maximal oxygen consumption and a
lowering of the respiratory quotient indicate that dietary carnitine has the potential to stimulate
lipid metabolism. Treatment with L-carnitine also has been shown to induce a significant
postexercise decrease in plasma lactate, which is formed and used continuously under fully
aerobic conditions. Data from preliminary studies have indicated that L-carnitine
supplementation can attenuate the deleterious effects of hypoxic training and speed up recovery
from exercise stress. Recent data have indicated that L-carnitine plays a decisive role in the
prevention of cellular damage and favorably affects recovery from exercise stress. Uptake of Lcarnitine by blood cells may induce at least three mechanisms: 1) stimulation of hematopoiesis,
2) a dose-dependent inhibition of collagen-induced platelet aggregation, and 3) the prevention
of programmed cell death in immune cells. As recently shown, carnitine has direct effects in
regulation of gene expression (i.e., carnitine-acyltransferases) and may also exert effects via
modulating intracellular fatty acid concentration. Thus there is evidence for a beneficial effect
of L-carnitine supplementation in training, competition, and recovery from strenuous exercise
and in regenerative athletics.
Correspondence to: Heidrun Karlic, PhD, Ludwig Boltzmann Institute for Leukemia Research and Hematology,
Hanusch Hospital, H. Collinstr. 30, A-1140 Vienna, Austria.


Dietary supplements to improve performance are familiar to many athletes.

Manufacturers more or less aggressively claim that the substances improve the
performance of athletes (i.e., act as ergo- genic aids) and/or speed up their recovery
from exercise. Most of these claims are purely speculative and based on
assumptions about how the dietary supplement influencesmetabolism. The
substance L-carnitine has been particularly popular as a potential ergogenic aid
energy.1,2 For a scheme, the reader isreferred to Figure 1.
L-carnitine was first discovered in muscle extracts by two Russian
scientists3 who
word carnis (flesh or meat). Its chemical structure was establishedin 1927, and in
published,4 which triggered numerousstudies on the physiological functions of the
chemical. In 1959 Fritz showed that carnitine increases long-chain fatty oxidation
heart.5 Another
name for Lcarnitine wasvitamin BT (T tenebrio) because the
larva of black beetle Tenebrio molitor (Tenebrionidae,Coleoptera)
requires Lcarnitine as a growth factor in addition to folic acid and other known B vitamins.
Considering the chemical structure, the choline-like metabolite L-carnitine (3-hydroxy-4N,N,Ntrimethylaminobutyrate,
acid ortrimethylamino- -hydroxybutyric acid) is a quaternary amine. In phrenic nerve diaphra
gm preparations, its effect,namely
induction of tetanic fade, can be reduced by addition of choline.6

FIG. 1. Role of L-carnitine in oxidative metabolism. L-carnitines primary function (blue arrows) is to shuttle fatty acids
CPT-I. CPT-II mediates the further progression toward -oxidation. Carnitines secondary function affectsthe CoASH/CoA ratio. CoASH is a two-carbon compound; CoA is a vitamin B
derivative. Supplemental L-carnitine can react with some of the excess CoASH groups that accu- mulate during strenous
exercise, thereby producing acetylcarnitine. This lowers the CoASH/CoA ratio, which in turn activates the enzyme PDH. PDH
causes some pyruvate to be converted to CoASH as opposed to lactic acid. Less lactic acid can mean delayed fatigue. Further, Lcarnitine
free CoA is released. Free CoA is necessary for continuous operation of the
Krebs cycle. Moreover,stimulating PDH enhances flow through the Krebs cycle; as a consequence, maximum oxygen capacity
(the capacity for aerobicregeneration of adenosine triphosphate) is increased. Together with a decreased respiratory quotient (the
quotient of exhaled CO2 equivalents per inhaled O2), this can mean increased exercise performance. CoA, coenzyme; CoASH,
CoASH, acetyl coenzyme A; CPT, carnitine palmi- toyltransferase; PDH, pyruvate dehydrogenase.

The function that has been investigated most thoroughly scientifically is the carnitinedependenttransport of fatty acids through the inner mitochondrial membrane. Other

functions ofL-carnitine are the preservation of membrane integrity,
the stabilization of a physiologic coenzyme A (CoA) acetyl-CoA (coASH) ratio in
mitochondria, and the reduction of lactate pro- duction.7,8 In vitro investigations
notion that Lcarnitine is ableto inhibit apoptosis (programmed
cell death)9 11 (Figure 2).

The intracellular homeostasis of carnitine is controlled by different membrane

transporters. The organic cation transporters (OCTNs), in particular OCTN2,
important,operate on intestinal absorption and renal reabsorption of L-carnitine and
play a major role in tissue distribution and varia- tions in transport rates. Inborn or
acquired defects on this carnitine transport mechanism lead to primary or
secondary carnitine deficiency. The OCTN2 mRNA content of cells is reduced
with aging12 and by oxygen radicals.13 OCTN2 is directly inhibited by several agents
and substances known to induce systemic carnitine deficiency.
Secondary carnitine deficiency is often seen in patients on regular
hemodialysis,14 with metabolic disorders, and in pregnancy.15
L-carnitine, widely available over the counter, is also favored among athletes. Rumors
the Italian national soccer team to win the world championship in 1982 contributed
immensely to its popularity. The most important claim relates to the role of carnitine
metabolism. L-carnitine
is often advertized to improve fat metabolism, reducefat mass, and
increase muscle mass. In other words, the substance is portrayed as
burner. Therefore, carnitine is often recommended for conditions in which
weight loss is indicated. Endurance athletes use carnitine to increase the oxidation of
fat during exercise and spare muscle glycogen. This review critically examines whether
the claims associated with L-carnitine arejustified.


L-carnitine plays an important role in fat metabolism. In the overnight-fasted state,
of low to moderate intensity, longchain fatty acids represent up to
80% of the energy sources. The best described function of L-carnitine is in its
role as a cofactor of carnitine, acyltransferases transporting long-chain fatty acids
across the mitochondrial inner membrane.21 In the absence of L-carnitine, the inner
mitochondrial membrane would be impermeable to long-chain fatty acids and fatty acylCoA esters. Once inside the mitochondria,these compounds can be degraded to acety
l-CoA through a process known as
oxidation. Carnitinealso plays a decisive role in maintaining the acetyl CoA/CoA ratio in
the cell. During high-intensity exercise, there is a large production of acetyl-CoA. This
increase in turn inhibits the pyruvate dehydrogenase (PDH) complex and reduces

flux through the PDH complex.22 As a consequence,acetyl-CoA gives rise to lactate.

Acetyl-CoA reacts with free carnitine to form acetyl-carnitine andCoA.

Carnitine therefore may supress the accumulation of lactic acid,




exercise performance. This has been confirmed in several studies, which are summarized in Table I. Results from a
pilot study in patients with the human immuno- deficiency virus receiving nucleoside analog therapy have suggested that L-carnitine may be helpful for patients who have nucleoside analogrelated lactic acidosis with blood


higher than 10mM/L.23 Sweeney et al.24 showed that addition of


carnitine may improve the quality of platelet concentratesthat

are stored beyond 5 d by providing better pH preservation, less
glucose consumption, and less lactategeneration.

Historically, skeletal muscle was seen mainly as the site of lactate production during
associated with insufficient muscle oxygenation and consequently
fatigue. Later, it was recognized that skeletal muscles not only play
an important role in lactateproduction but also in lactate clearance, and this improved
understanding has led to a renewed interest in the metabolic fate of lactate in skeletal
muscle and other tissues. Tracing studies using radioactive labeled lactate have shown
that skeletal muscle extracts lactate from the circulation despite a substantial net lactate
release, and that skeletal muscle has a large capacity for lactate oxidation; these

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