Binding of Ca2+ influences susceptibility of laminin to proteolytic digestion and interactions between domain-specific laminin fragments.
Ca2+ was found to influence the patterns of limit digests of laminin obtained with various neutral proteases. In the presence of Ca2+, larger fragments were obtained from the central part of laminin than in its absence. This was interpreted as being due to a stabilization of the central short-arm domains of laminin by bound Ca2+. When proteolytic fragments were tested for their ability to aggregate, only large fragments containing intact short arms were active, indicating an important role for these domains in laminin self-aggregation.
Paulsson
M
M
Department of Biophysical Chemistry, University of Basel, Switzerland.
Saladin
K
K
Landwehr
R
R
D002118:Calcium / Q000378:metabolism / Q000494:pharmacology*; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D005341:Fibrinolysin; D007797:Laminin / Q000378:metabolism*; D008970:Molecular Weight; D010196:Pancreatic Elastase; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism; D011485:Protein Binding
D007797:Laminin; D010446:Peptide Fragments; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D005341:Fibrinolysin; D002118:Calcium