Abstract:
:Guinea pig VIP differs from VIP of several mammals by its amino acids in positions 5, 9, 19 and 26. We tested a) its ability to occupy VIP receptors in liver and lung membranes of rat and guinea pig and in the human lymphoblastic SUP-T1 cell line and b) the ensuing adenylate cyclase stimulation. In liver and lung membranes from rat, guinea pig VIP was less potent than common VIP to occupy high and low affinity VIP receptors. In rat liver both VIP activated adenylate cyclase mostly through high affinity receptors. In rat lung, guinea pig VIP activated the enzyme mostly through high affinity receptors and was less efficient than common VIP acting through both classes of receptors. In guinea pig liver and lung membranes, binding inhibition curves were steeper than with rat preparations and adenylate cyclase appeared to be mostly activated through high affinity VIP receptors in liver and through both classes of receptors in lung. On human lymphoblastic SUP-T1 membranes both VIP were equally potent and efficient to inhibit tracer binding and activate adenylate cyclase.
journal_name
Peptidesjournal_title
Peptidesauthors
Cauvin A,Buscail L,Gourlet P,De Neef P,Robberecht P,Yanaihara N,Christophe Jdoi
10.1016/0196-9781(91)90180-wsubject
Has Abstractpub_date
1991-01-01 00:00:00pages
139-43issue
1eissn
0196-9781issn
1873-5169pii
0196-9781(91)90180-Wjournal_volume
12pub_type
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