Category: ECM

Guide to the extracellular matrix, anchor, and adhesion proteins 2nd Ed

Edited by Thomas Kreis and Ronald Vale (1999), A Sambrook & Tooze Publication At Oxford University press.

Part 1 Cytoskeleton-associated anchor and signal transduction proteins

Introduction

Linkers to actin filaments

  • aciculin
  • alpha-actinins
  • adducin
  • ankryns
  • calpains (EC 3.4.22.17)
  • alpha-catenin
  • cysteine-rich protein family
  • dystrophin/utrophin
  • ERM proteins: ezrin, radixin, and moesin
  • focal adhesion kinase (FAK)
  • paxillin
  • plakoglobin, beta-catenin, and the ARM family
  • ponticulin
  • p58gag
  • p130CAS
  • pp60c-src
  • 43K-rapsyn
  • Rho GTPase family (overview of family)
  • Rho
  • Rac
  • Cdc42
  • spectrins
  • talin
  • tensin
  • VASP
  • vinculin
  • zyxin

Linkers to intermediate filaments

  • desmocalmin
  • desmoplakins
  • pemphigoid antigens
  • plectin

Tight junction proteins

  • cingulin
  • symplekin
  • ZO-1 and ZO-2

Part 2 Cell adhesion and cell-cell contact proteins

  • Introduction
  • The Ig superfamily of adhesion molecules
  • cadherin/catenin-mediated signal transduction
  • signaling via integrins
  • ADAMs
  • cadherins
  • CCAM and other CEA-related CAMs
  • CD2/LFA-2
  • CD44
  • cell surface galactosyltransferase
  • chemokine receptors
  • c-Kit receptor tyrosine kienase – kit ligand/stem cell factor
  • connexins
  • contact site A
  • DCC family
  • dystroglycan
  • beta3-endoxin
  • Ep-CAM (epithelial cell adhesion molecule)
  • fascilin I
  • fascilin II
  • Fascilin III
  • Integrins
  • integrin-associated proteins
  • Intercellular adhesion molecules (ICAMs)
  • glypicans
  • limbic system-associated membrane protein
  • Leucine-rich repeat family
  • LFA-1
  • MAdCAM-1
  • Mannose binding proteins (MBP)
  • MHC class I and II
  • Myelin sheath proteins: Overview, Myellin-associated glycoproteins (MAG), myslin basic protein (MBPs), myelin oligodendrocyte glycoprotein (MOG), peripheral myelin protein 22 (PM22_, protein zero (P0), protelipid proteins (lipophilins)
  • Neural cell adhesion molecule (NCAM)
  • Neural cell recognition molecule F11 (contactin)
  • Neural cell recognition molecule L1
  • Neurofascin
  • Neuroglian
  • Neurotactin
  • Notch/delta/serrate
  • NgCAM-related cell adhesion molecule (NrCAM)
  • Occludin
  • PECAM-1/CD31
  • PH-20
  • Platelet GP Ib-IX-V complex
  • Selectins
  • Selectin ligands
  • sevenless and bride of sevenless
  • syndecans
  • TAG-1/axonin-1
  • TCR/CD3 complexes and the CD4 and CD8 co-receptors
  • tetraspans
  • Unc-5 family
  • VCAM-1
  • V-V-C2-C2-C2 CAMs
  • yeast sexual agglutinins

Part 3 ECMs and their receptors

Introduction

Modules in ECM and adhesion molecules

Proteoglycans

ECM modules

  • aggrecan
  • agrin
  • biglycan (BGN)
  • bone sialoprotein (BSP)
  • cartilage matrix protein
  • Cat-301 proteoglycan
  • cholinesterases
  • collagens: overview of the family, fibrillar collagens, FACIT collagens, short chain collagens, basement membrane collagens, multiplexins, collagen with transmembrane domains – MACITs, other collagen
  • decorin (DCN)
  • egg zona pellucida glycoproteins
  • elastin
  • fibrinogen/fibrin
  • fibromodulin
  • fibronectins
  • fibulins
  • hyaluronan, hyaluronan synthase, and hyaluronan-binding proteins
  • laminins
  • link protein
  • mucins
  • nectinepsin
  • netrins
  • nidogen
  • osteopontin
  • osteoprotegerin
  • perlecan
  • reelin
  • sea urchin ECM molecules
  • semaphorins
  • SPARC (osteonectin, BM40)
  • sponge ECM adhesion proteins
  • tenascins
  • thrombospondins
  • versican
  • vitronectin
  • von Willebrand factor

ECM proteinases

  • ECM proteineases
  • astacin/tolloid proteinases
  • lysosomal proteinases
  • matrix metalloproteinases
  • Collagenase (MMPs 1, 8, 13, and 18)
  • stromelysins 1 and 2 (MMPs 3 and 10)
  • Gelatinases (MMPs 2 and 9)
  • Matrylisin (MMP 7)
  • Membrane-type MMPs (MMPs 14, 15, 16, and 17)
  • Other MMPs (MMPs 11, 12, 19, and 20)
  • Tissue inhibitors of metalloproteinases (TIMPs)
  • Neutrophil elastase and cathepsin G
  • plasminogen
  • plasminogen activator inhibitors
  • tissue-type plasminogen activator (tPA)
  • urokinase-type plasminogen activator (uPA) and its receptor (uPAR)

Apakah basement membrane?

Basement membrane (BM) adalah matriks ekstraseluler tipis, sebagian besar terdiri dari protein, glikoprotein, dan glikosaminoglikan. Lebih khusus lagi, BM terutama terdiri dari: (CSH, SD)

  • kolagen tipe IV
  • laminin
  • entactin/nidogen
  • perlecan (heparan sulfate proteoglycan)

Namun, BM juga mengandung berbagai faktor pertumbuhan dan molekul lainnya.

With the use of the electron microscope in glutaraldehyde-fixed and heavy-metal-impregnated thin sections, the BM can be divided into two distinct parts:

  1. lamina lucida, immediately adjacent to the parenchymal cells
  2. lamina densa, right beneath lamina lucida.

This morphology has been questioned by studies using rapid freeze-substitution technique, in which the BMs appear solely as lamina densa (Histo, Micros).

It must be noted that although the basic ultrastructure of the BM is relatively identical in all tissues, differences do exist. This heterogeneity derives partly from the several trimer combinations of the respective laminin and type IV collagen chains.

Setidaknya ada 16 laminin dan kolagen tipe IV isoform saat ini telah diketahui [GS, CSH]. Selain itu, heterogenitas juga disumbang oleh perbedaan protein minor dan karbohidrat spesifik jaringan. Perbedaan ini dapat menjelaskan peran yang berbeda dari BM di setiap jaringan.

BM bersentuhan dengan sel epitelial dan endotelial, lemak, otot polos dan sel Schwann, dal lain-lain yang muncul dalam berbagai cara.

  1. They provide an intermediate adhesion area between parenchymal cells and the interstitial matrix.
  2. They act as a molecular filter, regulating the passage of substances within it, mostly due to the glycosaminoglycans.
  3. They hold an important role in cellular organization and differentiation, through mutual interaction between cell surface receptors and adjacent ECM components.

Retype from: Colorectal Cancer and Basement Membranes: Clinicopathological Correlations