摘要
Sea urchin petaloid coelomocytes efectuate the coting pathway by undergoing a rapid and dymamic cellular transfomation that leads to cellular adhesion and wounds closure.We have identified high levels of activity of aylsulfatase(Ars)associated with coelomocytes of the sea urchin ytechimu varieganus (Lamarck,1816).Ars activity was extracted from clotted coelomocytes with EDTA and showed high levels of activity up to a 1:100 dilution Clot fomation from isolated coelomic fuid was significantly inhbited by the ARS inhibitor,p-nito-phenyl phosphate.Ars activity was collected by 80%ethanol precipitation,a diagnostic test previously used in Ars isolation Cellular extraction studies in the presence and absence of the non-ionic detergent Tniton X-100 indicated that some Ars activity was present intacellularly.possibly in intacellular membrame-bound compart-ments,however the majonity of Ars activity was extracted from the extracellular coelomocyte membrane.Poly-clonal anti-sea urchin embryo Ars antibodies recognized a single protein band with an approximate molecular weight of 75 kDa on westem blots.Immumofluorescence using the anti-sea urchin Ars antibody revealed an in-tacellular and extacelular staining of Ars in both petalloid and filopodial coelomocytes.Taken together,these data indicate that coelomocyte Ars might be involved in cell-to-cell croslinking of suface sulfated polysaccha-nides vital for clot fomation.
