Tripeptidyl peptidase I

Tripeptidyl peptidase I

Tripeptidyl peptidase I, also known as TPP1, is a human gene.cite web | title = Entrez Gene: TPP1 tripeptidyl peptidase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1200| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.cite web | title = Entrez Gene: TPP1 tripeptidyl peptidase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1200| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Mole SE, Mitchison HM, Munroe PB |title=Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5. |journal=Hum. Mutat. |volume=14 |issue= 3 |pages= 199–215 |year= 1999 |pmid= 10477428 |doi= 10.1002/(SICI)1098-1004(1999)14:3<199::AID-HUMU3>3.0.CO;2-A |doilabel=10.1002/(SICI)1098-1004(1999)14:3199::AID-HUMU33.0.CO;2-A
*cite journal | author=Dawson G, Cho S |title=Batten's disease: clues to neuronal protein catabolism in lysosomes. |journal=J. Neurosci. Res. |volume=60 |issue= 2 |pages= 133–40 |year= 2000 |pmid= 10740217 |doi=
*cite journal | author=Hofmann SL, Atashband A, Cho SK, "et al." |title=Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2). |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 423–37 |year= 2003 |pmid= 12125808 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Page AE, Fuller K, Chambers TJ, Warburton MJ |title=Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption. |journal=Arch. Biochem. Biophys. |volume=306 |issue= 2 |pages= 354–9 |year= 1993 |pmid= 8215436 |doi=
*cite journal | author=Sleat DE, Donnelly RJ, Lackland H, "et al." |title=Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. |journal=Science |volume=277 |issue= 5333 |pages= 1802–5 |year= 1997 |pmid= 9295267 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Liu CG, Sleat DE, Donnelly RJ, Lobel P |title=Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis. |journal=Genomics |volume=50 |issue= 2 |pages= 206–12 |year= 1998 |pmid= 9653647 |doi= 10.1006/geno.1998.5328
*cite journal | author=Rawlings ND, Barrett AJ |title=Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis. |journal=Biochim. Biophys. Acta |volume=1429 |issue= 2 |pages= 496–500 |year= 1999 |pmid= 9989235 |doi=
*cite journal | author=Vines DJ, Warburton MJ |title=Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I. |journal=FEBS Lett. |volume=443 |issue= 2 |pages= 131–5 |year= 1999 |pmid= 9989590 |doi=
*cite journal | author=Sleat DE, Gin RM, Sohar I, "et al." |title=Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder. |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1511–23 |year= 1999 |pmid= 10330339 |doi=
*cite journal | author=Junaid MA, Wu G, Pullarkat RK |title=Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis. |journal=J. Neurochem. |volume=74 |issue= 1 |pages= 287–94 |year= 2000 |pmid= 10617131 |doi=
*cite journal | author=Ezaki J, Takeda-Ezaki M, Oda K, Kominami E |title=Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 3 |pages= 904–8 |year= 2000 |pmid= 10679303 |doi= 10.1006/bbrc.2000.2207
*cite journal | author=Haines JL, Boustany RM, Alroy J, "et al." |title=Chromosomal localization of two genes underlying late-infantile neuronal ceroid lipofuscinosis. |journal=Neurogenetics |volume=1 |issue= 3 |pages= 217–22 |year= 2000 |pmid= 10737126 |doi=
*cite journal | author=Ezaki J, Takeda-Ezaki M, Kominami E |title=Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase. |journal=J. Biochem. |volume=128 |issue= 3 |pages= 509–16 |year= 2000 |pmid= 10965052 |doi=
*cite journal | author=Lin L, Sohar I, Lackland H, Lobel P |title=The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. |journal=J. Biol. Chem. |volume=276 |issue= 3 |pages= 2249–55 |year= 2001 |pmid= 11054422 |doi= 10.1074/jbc.M008562200
*cite journal | author=Lam CW, Poon PM, Tong SF, Ko CH |title=Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis. |journal=Am. J. Med. Genet. |volume=99 |issue= 2 |pages= 161–3 |year= 2001 |pmid= 11241479 |doi=
*cite journal | author=Zhong N, Moroziewicz DN, Ju W, "et al." |title=Heterogeneity of late-infantile neuronal ceroid lipofuscinosis. |journal=Genet. Med. |volume=2 |issue= 6 |pages= 312–8 |year= 2001 |pmid= 11339651 |doi=

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