Léptin

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1ax8

Leptin
	Wangun protéin obés léptin-E100.
Identifiers
Symbol	Léptin
Pfam	PF02024
Pfam clan	CL0053
InterPro	IPR000065
SCOPe	1ax8 / SUPFAM
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1ax8

LEP
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1AX8
Identifiers
Aliases	LEP, LEPD, OB, OBS, leptin
External IDs	OMIM: 164160 HomoloGene: 193 GeneCards: LEP
Gene ontology
Molecular function	• hormone activity; • peptide hormone receptor binding; • receptor binding;
Cellular component	• sitoplasma; • extracellular region; • extracellular space;
Biological process	• regulation of protein phosphorylation; • response to dietary excess; • cellular response to retinoic acid; • positive regulation of developmental growth; • negative regulation of glucagon secretion; • placenta development; • cardiac muscle hypertrophy; • regulation of angiogenesis; • prostaglandin secretion; • regulation of intestinal cholesterol absorption; • T cell differentiation; • positive regulation of reactive oxygen species metabolic process; • central nervous system neuron development; • Ritme sirkadian; • positive regulation of ion transport; • Angiogenesis; • glucose metabolic process; • positive regulation of peroxisome proliferator activated receptor signaling pathway; • positive regulation of hepatic stellate cell activation; • regulation of endothelial cell proliferation; • intestinal absorption; • response to ethanol; • negative regulation of autophagy; • positive regulation of p38MAPK cascade; • positive regulation of protein kinase B signaling; • negative regulation of metabolic process; • negative regulation of vasoconstriction; • glucose homeostasis; • regulation of insulin secretion; • regulation of steroid biosynthetic process; • insulin secretion; • regulation of natural killer cell activation; • regulation of fat cell differentiation; • response to vitamin E; • response to nutrient levels; • bone mineralization involved in bone maturation; • positive regulation of T cell proliferation; • positive regulation of protein import into nucleus; • regulation of brown fat cell differentiation; • fatty acid beta-oxidation; • regulation of metabolic process; • hormone metabolic process; • positive regulation of MAPK cascade; • positive regulation of TOR signaling; • cellular response to L-ascorbic acid; • ovulation from ovarian follicle; • activation of protein kinase C activity; • Reproduksi seksual; • negative regulation of cartilage development; • response to nutrient; • negative regulation of glutamine transport; • leptin-mediated signaling pathway; • bile acid metabolic process; • female pregnancy; • negative regulation of apoptotic process; • cholesterol metabolic process; • positive regulation of follicle-stimulating hormone secretion; • negative regulation of transcription from RNA polymerase II promoter; • negative regulation of appetite; • regulation of protein localization to nucleus; • regulation of blood pressure; • negative regulation of glucose import; • leukocyte tethering or rolling; • negative regulation of lipid storage; • adipose tissue development; • positive regulation of insulin receptor signaling pathway; • bone growth; • positive regulation of JAK-STAT cascade; • glycerol biosynthetic process; • positive regulation of luteinizing hormone secretion; • fatty acid catabolic process; • regulation of gluconeogenesis; • response to estradiol; • intracellular signal transduction; • adult feeding behavior; • respons terhadap hipoksia; • regulation of natural killer cell proliferation; • eating behavior; • positive regulation of cytokine production; • regulation of cytokine production involved in inflammatory response; • regulation of nitric-oxide synthase activity; • response to activity; • cellular response to leptin stimulus; • regulation of cell cycle; • regulation of natural killer cell mediated cytotoxicity; • positive regulation of fat cell apoptotic process; • interleukin-6 secretion; • positive regulation of cell proliferation; • interleukin-8 secretion; • regulation of lipoprotein lipid oxidation; • positive regulation of phosphatidylinositol 3-kinase signaling; • signal transduction; • regulation of bone remodeling; • Q6556363; • negative regulation of appetite by leptin-mediated signaling pathway; • interleukin-12 production; • positive regulation of tumor necrosis factor production; • interleukin-6 production; • response to insulin; • tyrosine phosphorylation of STAT protein; • Fagositosis; • energy reserve metabolic process; • positive regulation of tyrosine phosphorylation of STAT protein; • regulation of receptor activity; • determination of adult lifespan; • regulation of lipid biosynthetic process; • positive regulation of cold-induced thermogenesis; • aorta development; • regulation of catalytic activity; • elastin metabolic process;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	3952
	n/a
	ENSG00000174697
	n/a
	P41159
	n/a
	NM_000230
	n/a
	NP_000221
	n/a
	Wikidata
View/Edit Human

‹ The template Infobox gene is being considered for merging. ›

Léptin (tina Yunani λεπτός leptos, "ipis") nyaéta hormon anu utamana dijieun ku sél adiposa jeung peujit leutik nu ngabantuan ngatur kasaimbangan énérgi ku ngahalangan lapar. Hormon ieu meta dina reséptor di hipotalamus.^[3] Dina obesitasna, sénsitipitas kana leptin jadi ngurangan (siga résisténsi insulin dina diabetes 2) anu balukarna henteu mampuh ngadeteksi kawareg najan simpenan énérni geus pon kitu ogé kadar léptinna.^[4]

Najan pangaturan simpenan lemak dianggap salaku fungsi utamana, léptin ogé boga peran dina prosés fisiologis séjénna,^[5] sakumaha kabukti ku loba loka sintésisna di saluareun sél lemak jeung sababaraha tipeu sél lian ti sél hipotalamik anu boga reséptor leptin. Pancén lianna ieu digarali kénéh. ^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

Pangaruh[édit | édit sumber]

Two white mice both with similar sized ears, black eyes, and pink noses: The body of the mouse on the left, however, is about three times the width of the normal-sized mouse on the right.

Babandingan beurit anu henteu bisa ngahasilkeun léptin, jadina obesitas, lapar, jeung létoy (kénca), jeung beurit normal (katuhu).

Perenah aksi: Léptin langsung bereaksi jeung reséptor léptin dina mémbran rupa-rupa sél dina waruga manusa, pon kitu oge vertebrata sacara umum. Reséptor leptin kaasup reséptor sitokin tipe I single-transmembrane-domain.^[12] Léptin ogé boga pancén jeung pangaruh ka hormon lianna, régulator énérgi, alajengna, léptin berinteraksi jeung hormon séjén jeung régulator énergi, langsung nyapih efek tina insulin, glukagon, faktor tumuwuh kawas insulin, hormon pertumbuhan, glukokortikoid, sitokin, jeung metabolit. ^[13]

Pungsi: Pungsi utama léptin nyaéta régulasi/pangaturan massa jaringan adiposa ngaliwatan pangaruh anu dimédiasi hipotalamus séntral dina lapar, pamakéan énérgi pangan, olah raga jeung kasaimbangan énérgi. Luareun uteuk, dina périfér awak, fungsi sekundér léptin nyaéta: modulasi pangaluaran énérgi, modulasi métabolisme antara fétal jeung maternal, ngaktipkeun sél imun, jeung paktor pertumbuhan.

Sajarah[édit | édit sumber]

Léptin kapanggih ku Jeffrey Freidman taun 1994sanggeus puluhan taun panalungtikan ku séjén lembaga ti 1950-an maké modél mencit obés.^[14]

Rujukan[édit | édit sumber]

↑ "Human PubMed Reference:".
↑ "Crystal structure of the obese protein leptin-E100". Nature 387 (6629): 206–09. May 1997. Bibcode 1997Natur.387..206Z. doi:10.1038/387206a0. PMID 9144295.
↑ "Drug Insight: the role of leptin in human physiology and pathophysiology – emerging clinical applications". Nat Clin Pract Endocrinol Metab 2 (6): 318–27. 2006. doi:10.1038/ncpendmet0196. PMID 16932309.
↑ "Advances in understanding the interrelations between leptin resistance and obesity". Physiology & Behavior 130: 157–69. May 2014. doi:10.1016/j.physbeh.2014.04.003. PMID 24726399.
↑ Article in "Mammalian Biology"
↑ "Weight-reducing effects of the plasma protein encoded by the obese gene". Science 269 (5223): 543–46. July 1995. Bibcode 1995Sci...269..543H. doi:10.1126/science.7624777. PMID 7624777.
↑ "Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks". Science 269 (5223): 546–49. July 1995. Bibcode 1995Sci...269..546C. doi:10.1126/science.7624778. PMID 7624778.
↑ "Effects of the obese gene product on body weight regulation in ob/ob mice". Science 269 (5223): 540–43. July 1995. Bibcode 1995Sci...269..540P. doi:10.1126/science.7624776. PMID 7624776.
↑ "Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects". Nat. Med. 1 (11): 1155–61. November 1995. doi:10.1038/nm1195-1155. PMID 7584987.
↑ "Evidence against either a premature stop codon or the absence of obese gene mRNA in human obesity". J. Clin. Invest. 95 (6): 2986–88. June 1995. doi:10.1172/JCI118007. PMC 295988. PMID 7769141. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=295988.
↑ "Serum immunoreactive-leptin concentrations in normal-weight and obese humans". N. Engl. J. Med. 334 (5): 292–95. 1996. doi:10.1056/NEJM199602013340503. PMID 8532024.
↑ "Leptin signaling in breast cancer: an overview". Journal of Cellular Biochemistry 105 (4): 956–64. 2008. doi:10.1002/jcb.21911. PMID 18821585.
↑ "Leptin: a review of its peripheral actions and interactions". Int. J. Obes. Relat. Metab. Disord. 26 (11): 1407–33. 2002. doi:10.1038/sj.ijo.0802142. PMID 12439643.
↑ "The Rockefeller University » Hospital Centennial". centennial.rucares.org. Diakses tanggal 2018-10-11.

Tutumbu kaluar[édit | édit sumber]

Leptin: uteuk anjeun, napsu jeung obesitas ku British Society of Neuroendocrinology
Leptin ku Colorado State University - ilustrasi hadé, ngan geus lila teu dimutahirkeun
Leptin di 3Dchem.com, pedaran jeung diagram wangunna

Artikel ieu mangrupa taratas, perlu disampurnakeun. Upami sadérék uninga langkung paos perkawis ieu, dihaturan kanggo ngalengkepan.

[1] "Human PubMed Reference:".

[pmid9144295-2] "Crystal structure of the obese protein leptin-E100". Nature 387 (6629): 206–09. May 1997. Bibcode 1997Natur.387..206Z. doi:10.1038/387206a0. PMID 9144295.

[pmid16932309-3] "Drug Insight: the role of leptin in human physiology and pathophysiology – emerging clinical applications". Nat Clin Pract Endocrinol Metab 2 (6): 318–27. 2006. doi:10.1038/ncpendmet0196. PMID 16932309.

[4] "Advances in understanding the interrelations between leptin resistance and obesity". Physiology & Behavior 130: 157–69. May 2014. doi:10.1016/j.physbeh.2014.04.003. PMID 24726399.

[5] Article in "Mammalian Biology"

[pmid7624777-6] "Weight-reducing effects of the plasma protein encoded by the obese gene". Science 269 (5223): 543–46. July 1995. Bibcode 1995Sci...269..543H. doi:10.1126/science.7624777. PMID 7624777.

[pmid7624778-7] "Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks". Science 269 (5223): 546–49. July 1995. Bibcode 1995Sci...269..546C. doi:10.1126/science.7624778. PMID 7624778.

[pmid7624776-8] "Effects of the obese gene product on body weight regulation in ob/ob mice". Science 269 (5223): 540–43. July 1995. Bibcode 1995Sci...269..540P. doi:10.1126/science.7624776. PMID 7624776.

[pmid7584987-9] "Leptin levels in human and rodent: measurement of plasma leptin and ob RNA in obese and weight-reduced subjects". Nat. Med. 1 (11): 1155–61. November 1995. doi:10.1038/nm1195-1155. PMID 7584987.

[pmid7769141-10] "Evidence against either a premature stop codon or the absence of obese gene mRNA in human obesity". J. Clin. Invest. 95 (6): 2986–88. June 1995. doi:10.1172/JCI118007. PMC 295988. PMID 7769141. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=295988.

[pmid8532024-11] "Serum immunoreactive-leptin concentrations in normal-weight and obese humans". N. Engl. J. Med. 334 (5): 292–95. 1996. doi:10.1056/NEJM199602013340503. PMID 8532024.

[pmid18821585-12] "Leptin signaling in breast cancer: an overview". Journal of Cellular Biochemistry 105 (4): 956–64. 2008. doi:10.1002/jcb.21911. PMID 18821585.

[Margetic-13] "Leptin: a review of its peripheral actions and interactions". Int. J. Obes. Relat. Metab. Disord. 26 (11): 1407–33. 2002. doi:10.1038/sj.ijo.0802142. PMID 12439643.

[14] "The Rockefeller University » Hospital Centennial". centennial.rucares.org. Diakses tanggal 2018-10-11.

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