PMID- 10329602
OWN - NLM
STAT- MEDLINE
DCOM- 19990603
LR  - 20190607
IS  - 0002-9440 (Print)
IS  - 0002-9440 (Linking)
VI  - 154
IP  - 5
DP  - 1999 May
TI  - Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell
      adhesion.
PG  - 1489-501
AB  - The ADAMs (A disintegrin and metalloprotease) comprise a family of
      membrane-anchored cell surface proteins with a putative role in cell-cell and/or 
      cell-matrix interactions. By immunostaining, ADAM 12 (meltrin alpha) was
      up-regulated in several human carcinomas and could be detected along the tumor
      cell membranes. Because of this intriguing staining pattern, we investigated
      whether human ADAM 12 supports tumor cell adhesion. Using an in vitro assay using
      recombinant polypeptides expressed in Escherichia coli, we examined the ability
      of individual domains of human ADAM 12 and ADAM 15 to support tumor cell
      adhesion. We found that the disintegrin-like domain of human ADAM 15 supported
      adhesion of alphavbeta3-expressing A375 melanoma cells. In the case of human ADAM
      12, however, recombinant polypeptides of the cysteine-rich domain but not the
      disintegrin-like domain supported cell adhesion of a panel of carcinoma cell
      lines. On attachment to recombinant polypeptides from the cysteine-rich domain of
      human ADAM 12, most tumor cell lines, such as MDA-MB-231 breast carcinoma cells, 
      were rounded and associated with numerous actin-containing filopodia and used a
      cell surface heparan sulfate proteoglycan to attach. Finally, we demonstrated
      that authentic full-length human ADAM 12 could bind to heparin Sepharose.
      Together these results suggest a novel role of the cysteine-rich domain of ADAM
      12 -- that of supporting tumor cell adhesion.
FAU - Iba, K
AU  - Iba K
AD  - Institute of Molecular Pathology, University of Copenhagen, Copenhagen, Denmark.
FAU - Albrechtsen, R
AU  - Albrechtsen R
FAU - Gilpin, B J
AU  - Gilpin BJ
FAU - Loechel, F
AU  - Loechel F
FAU - Wewer, U M
AU  - Wewer UM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Pathol
JT  - The American journal of pathology
JID - 0370502
RN  - 0 (Heparan Sulfate Proteoglycans)
RN  - 0 (Membrane Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - EC 3.4.24.- (ADAM Proteins)
RN  - EC 3.4.24.- (ADAM12 Protein)
RN  - EC 3.4.24.- (Adam12 protein, mouse)
RN  - K848JZ4886 (Cysteine)
SB  - AIM
SB  - IM
MH  - ADAM Proteins
MH  - ADAM12 Protein
MH  - Carcinoma/*pathology
MH  - Cell Adhesion/physiology
MH  - Cysteine/*analysis
MH  - Heparan Sulfate Proteoglycans/physiology
MH  - Humans
MH  - Immunohistochemistry
MH  - Membrane Proteins/*chemistry
MH  - Muscle Proteins/*chemistry
MH  - Neoplasm Proteins/*chemistry
MH  - *Protein Structure, Tertiary
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Tumor Cells, Cultured
MH  - Up-Regulation
PMC - PMC1866592
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - S0002-9440(10)65403-X [pii]
AID - 10.1016/s0002-9440(10)65403-x [doi]
PST - ppublish
SO  - Am J Pathol. 1999 May;154(5):1489-501. doi: 10.1016/s0002-9440(10)65403-x.