MMP16

MMP16

Matrix metallopeptidase 16 (membrane-inserted), also known as MMP16, is a human gene.cite web | title = Entrez Gene: MMP16 matrix metallopeptidase 16 (membrane-inserted)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4325| accessdate = ]

PBB_Summary
section_title =
summary_text = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene produces at least two transcripts, one which encodes a membrane-bound form and another a soluble form of the protein. Both forms of the protein activate MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16.cite web | title = Entrez Gene: MMP16 matrix metallopeptidase 16 (membrane-inserted)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4325| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=
*cite journal | author=Takino T, Sato H, Shinagawa A, Seiki M |title=Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 23013–20 |year= 1995 |pmid= 7559440 |doi=
*cite journal | author=Andersson B, Wentland MA, Ricafrente JY, "et al." |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138
*cite journal | author=Mattei MG, Roeckel N, Olsen BR, Apte SS |title=Genes of the membrane-type matrix metalloproteinase (MT-MMP) gene family, MMP14, MMP15, and MMP16, localize to human chromosomes 14, 16, and 8, respectively. |journal=Genomics |volume=40 |issue= 1 |pages= 168–9 |year= 1997 |pmid= 9070935 |doi= 10.1006/geno.1996.4559
*cite journal | author=Shofuda K, Yasumitsu H, Nishihashi A, "et al." |title=Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 9749–54 |year= 1997 |pmid= 9092507 |doi=
*cite journal | author=Yu W, Andersson B, Worley KC, "et al." |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=
*cite journal | author=Sato H, Tanaka M, Takino T, "et al." |title=Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization. |journal=Genomics |volume=39 |issue= 3 |pages= 412–3 |year= 1997 |pmid= 9119382 |doi= 10.1006/geno.1996.4496
*cite journal | author=Matsumoto S, Katoh M, Saito S, "et al." |title=Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA. |journal=Biochim. Biophys. Acta |volume=1354 |issue= 2 |pages= 159–70 |year= 1998 |pmid= 9396633 |doi=
*cite journal | author=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi=
*cite journal | author=Iida J, Pei D, Kang T, "et al." |title=Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 18786–94 |year= 2001 |pmid= 11278606 |doi= 10.1074/jbc.M010053200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Jung M, Römer A, Keyszer G, "et al." |title=mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue. |journal=Prostate |volume=55 |issue= 2 |pages= 89–98 |year= 2003 |pmid= 12661033 |doi= 10.1002/pros.10194
*cite journal | author=Takino T, Koshikawa N, Miyamori H, "et al." |title=Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases. |journal=Oncogene |volume=22 |issue= 30 |pages= 4617–26 |year= 2003 |pmid= 12879005 |doi= 10.1038/sj.onc.1206542
*cite journal | author=Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY |title=The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4260–8 |year= 2004 |pmid= 14645246 |doi= 10.1074/jbc.M311569200
*cite journal | author=Lang R, Braun M, Sounni NE, "et al." |title=Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features. |journal=J. Mol. Biol. |volume=336 |issue= 1 |pages= 213–25 |year= 2004 |pmid= 14741217 |doi=
*cite journal | author=Shofuda T, Shofuda K, Ferri N, "et al." |title=Cleavage of focal adhesion kinase in vascular smooth muscle cells overexpressing membrane-type matrix metalloproteinases. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 5 |pages= 839–44 |year= 2004 |pmid= 15044209 |doi= 10.1161/01.ATV.0000126680.78500.4c
*cite journal | author=Wang SC, Lien HC, Xia W, "et al." |title=Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2. |journal=Cancer Cell |volume=6 |issue= 3 |pages= 251–61 |year= 2004 |pmid= 15380516 |doi= 10.1016/j.ccr.2004.07.012
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, "et al." |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужно решить контрольную?

Look at other dictionaries:

  • Матриксная металлопротеиназа 16 — Структура белка MMP16 …   Википедия

  • Matrix metalloproteinase — Cell surface associated MT1 MMP (MMP14), Green fluorescent protein (GFP) fused to the C term produces a signal on the surface of the cell[1] Matrix metalloproteinases (MMPs) are zinc dependent endopeptidases; other family members are adamalysins …   Wikipedia

  • Матриксные металлопротеиназы — (MMP) семейство внеклеточных цинк зависимых эндопептидаз, способных разрушать все типы белков внеклеточного матрикса. Играют роль в ремоделировании тканей, ангиогенезе, пролиферации, миграции и дифференциации клеток, апоптозе, сдерживании роста… …   Википедия

  • Metalloendopeptidase — A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. External links MeSH Metalloendopeptidase 3.4.21 24: Endopeptidase …   Wikipedia

  • Collagenase — matrix metallopeptidase 1 (interstitial collagenase) Identifiers Symbol MMP1 Entrez 4312 HUGO …   Wikipedia

  • ADAM17 — ADAM metallopeptidase domain 17 PDB rendering based on 1bkc …   Wikipedia

  • Neprilysin — Membrane metallo endopeptidase The structure of the neprilysin ectodomain in complex with a zinc chelating inhibitor. The zinc atom is shown as a gray sphere and the inhibitor is shown in green. Rendering based on 1r1h …   Wikipedia

  • Pregnancy-associated plasma protein A — Pregnancy associated plasma protein A, pappalysin 1 Identifiers Symbols PAPPA; ASBABP2; DIPLA1; IGFBP 4ase; PAPA; PAPP A; PAPPA1 External IDs …   Wikipedia

  • MMP14 — Matrix metallopeptidase 14 (membrane inserted) PDB rendering based on 1bqq …   Wikipedia

  • MMP1 — Matrix metallopeptidase 1 (interstitial collagenase) PDB rendering based on 1ayk …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”