The interactions of alpha 2HS glycoprotein with metalloproteinases.
The objective of the present analyses was to determine whether matrix metalloproteinases interact with alpha 2HS glycoprotein, the human homologue of bovine fetuin. Alpha 2HS glycoprotein was incubated with metalloproteinases at 1:1 and 1:10 molar ratios. The serum glycoprotein was completely degraded by gelatinase-A and matrilysin at the higher enzyme concentration after an overnight incubation at 37 degrees C. The data show that gelatinase-A, matrilysin and gelatinase-B do interact with alpha 2HS glycoprotein and that gelatinase-B associates most tightly with the serum glycoprotein.
Ochieng
J
J
Meharry Medical College, Department of Biochemistry, Nashville TN 38208, USA.
Green
B
B
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D017364:Collagenases / Q000378:metabolism; D004792:Enzyme Precursors / Q000378:metabolism; D018093:Gelatinases / Q000378:metabolism; D006801:Humans; D020778:Matrix Metalloproteinase 2; D020783:Matrix Metalloproteinase 7; D020780:Matrix Metalloproteinase 9; D008666:Metalloendopeptidases / Q000378:metabolism*; D060749:alpha-2-HS-Glycoprotein
C556354:AHSG protein, human; D001798:Blood Proteins; D004792:Enzyme Precursors; D060749:alpha-2-HS-Glycoprotein; D017364:Collagenases; D018093:Gelatinases; D008666:Metalloendopeptidases; D020783:Matrix Metalloproteinase 7; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9