PMID- 10022829
OWN - NLM
STAT- MEDLINE
DCOM- 19990426
LR  - 20181113
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 4
DP  - 1999 Feb 15
TI  - Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to
      heparin, sulfatides, alpha-dystroglycan and several extracellular matrix
      proteins.
PG  - 863-70
AB  - The C-terminal G domain of the mouse laminin alpha2 chain consists of five
      lamin-type G domain (LG) modules (alpha2LG1 to alpha2LG5) and was obtained as
      several recombinant fragments, corresponding to either individual modules or the 
      tandem arrays alpha2LG1-3 and alpha2LG4-5. These fragments were compared with
      similar modules from the laminin alpha1 chain and from the C-terminal region of
      perlecan (PGV) in several binding studies. Major heparin-binding sites were
      located on the two tandem fragments and the individual alpha2LG1, alpha2LG3 and
      alpha2LG5 modules. The binding epitope on alpha2LG5 could be localized to a
      cluster of lysines by site-directed mutagenesis. In the alpha1 chain, however,
      strong heparin binding was found on alpha1LG4 and not on alpha1LG5. Binding to
      sulfatides correlated to heparin binding in most but not all cases. Fragments
      alpha2LG1-3 and alpha2LG4-5 also bound to fibulin-1, fibulin-2 and nidogen-2 with
      Kd = 13-150 nM. Both tandem fragments, but not the individual modules, bound
      strongly to alpha-dystroglycan and this interaction was abolished by EDTA but not
      by high concentrations of heparin and NaCl. The binding of perlecan fragment PGV 
      to alpha-dystroglycan was even stronger and was also not sensitive to heparin.
      This demonstrated similar binding repertoires for the LG modules of three
      basement membrane proteins involved in cell-matrix interactions and
      supramolecular assembly.
FAU - Talts, J F
AU  - Talts JF
AD  - Max-Planck-Institut fur Biochemie, Am Klopferspitz 18A, D-82152 Martinsried,
      Germany.
FAU - Andac, Z
AU  - Andac Z
FAU - Gohring, W
AU  - Gohring W
FAU - Brancaccio, A
AU  - Brancaccio A
FAU - Timpl, R
AU  - Timpl R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Heparan Sulfate Proteoglycans)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Sulfoglycosphingolipids)
RN  - 0 (fibulin)
RN  - 0 (fibulin 2)
RN  - 0 (laminin alpha 2)
RN  - 0 (nidogen)
RN  - 143972-95-6 (perlecan)
RN  - 146888-27-9 (Dystroglycans)
RN  - 151186-83-3 (laminin A)
RN  - 9005-49-6 (Heparin)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Binding, Competitive
MH  - Calcium-Binding Proteins/metabolism
MH  - Cytoskeletal Proteins/*metabolism
MH  - Dystroglycans
MH  - Extracellular Matrix Proteins/*metabolism
MH  - *Heparan Sulfate Proteoglycans
MH  - Heparin/*metabolism
MH  - Heparitin Sulfate/*metabolism
MH  - Kinetics
MH  - Laminin/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Mutagenesis, Site-Directed
MH  - Peptide Fragments/metabolism
MH  - Protein Binding
MH  - Proteoglycans/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Sulfoglycosphingolipids/*metabolism
PMC - PMC1171179
EDAT- 1999/02/18 00:00
MHDA- 1999/02/18 00:01
CRDT- 1999/02/18 00:00
PHST- 1999/02/18 00:00 [pubmed]
PHST- 1999/02/18 00:01 [medline]
PHST- 1999/02/18 00:00 [entrez]
AID - 10.1093/emboj/18.4.863 [doi]
PST - ppublish
SO  - EMBO J. 1999 Feb 15;18(4):863-70. doi: 10.1093/emboj/18.4.863.