Ciba Foundation Symposium 212 - Plasminogen-Related Growth

A well timed quantity facing the evolutionary and structural hyperlinks among the clotting and fibrinolytic proteins and plasminogen-related progress elements. The position of person domain names for enzymatic proteins and plasminogen-related progress components is additionally comprehensively tested.

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J. F. Degen, unpublished results). The goal of this study was to see if Ron and HGFl/MSP are linked in this organism. It is too early to tell whether they are linked, but we have identified genomic clones. All we have to d o is get back to the UK MRC Human Genome Mapping Project Resource Centre here in England and get those clones. Gberardi: Did you isolate clones for HGPjSF and Met at the same time? FrieTner Depnn:W e don’t know yet whether we did o r not. We used mouse c D N A sequences t o probe the puffer fish library.

Rircbmier: What is the function of apolipoprotein (a)? I’. 1;riqner l > e ‘ p : High levels of apolipoprotein (a) in the b l ~ o dcorrelate with increased risks for atherosclerosis, and are found in plaques. T h e kringles vary in number in apolipoprotein (a), and from what I’ve heard it appears that the more kringles, the higher the risk ofatherosclerosis. U p t o 38 kringle domains have been found in apolipoprotein (a). However, its physiological role isn’t clear. W . Bircbmeier: Earlier o n y o u mentioned angiogenin, which is related t o ribonuclease (Palmer et a1 1986) .

First, HGFl/MSP does not bind to Sea. Second, we have been looking for the counterpart of Sea in a number of different living organisms for about five years now. We have cloned everything else but the mammalian counterpart of Sea. This doesn’t prove anything, admittedly, but just to show that we know how to look for genes, we have cloned seven homologues of Met in the extracellular domain. I am beginning to think that Sea doesn’t exist in mammals. Gherardi: The data would prove that even if a molecule should exist, it may still be difficult to find it.

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