Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.49 (reverse transcriptase)
 31,746 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The capability of rat pituitary cells to express receptors for pituitary adenylate cyclase activating polypeptide (PACAP) and VIP was evaluated by binding studies and measurement of adenylate cyclase activity on whole gland preparations and by reverse transcriptase-polymerase chain reaction (TR-PCR) using specific primers on preparations from isolated cell populations enriched in PRL- and GH-producing cells. Data obtained on whole gland preparations indicated that selective PACAP receptors (PACAP Type I) predominated. The mRNA coding for PACAP Type I and for the non-selective PACAP receptors Type II VIP2 (but not VIP1) were identified. The mRNA coding for four different spliced variants of the PACAP Type I receptor were detected. In PRL producing cells, three variants and the VIP2 mRNA were detected, whereas in GH-producing cells the mRNA coding for the variant having a 28-amino acid insert (termed HOP) in the third intracellular loop was the only present.
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PMID:Differential alternative splicing of PACAP receptor in pituitary cell subpopulations. 867 20

The SUP T1 lymphoblasts express an original subtype of VIP receptors characterized by a high affinity for the VIP analogue from lizard venom named helodermin, a preference for the neuropeptide PACAP-38 over PACAP-27 and VIP, and an extremely low affinity for secretin. The molecular cloning of that receptor revealed its identity with the VIP2 receptor subtype first cloned in rat and mouse tissues. The access to selective probes permits the detection of the mRNA coding for the VIP2 receptor by Northern blot, reverse transcriptase-polymerase chain reaction (RT-PCR) and in situ hybridization. These highly selective and sensitive techniques identify the cell types that are equipped to synthesize the receptor but do not prove that the receptor is indeed efficiently expressed at the cell surface. VIP2 mRNA was detected in selected areas of the brain different from that expressing the classical VIP1 receptor, in pituitary, in pineal, in pancreatic islets, in testes and ovary. It was also detected in the stomach, in the thymus and in spleen and in T lymphoblastic cell lines. A systematic screening of the immunocompetent cells must still be performed.
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PMID:Characterization of the VIP receptor from SUP T1 lymphoblasts. 879 Jul 81

In both functional and radioligand binding studies of gastric smooth muscle from rabbit and guinea pig, vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) show equal potency indicating that the receptor type is either a VIP1/PACAP2 or a VIP2/PACAP3 receptor. We have characterized the VIP/PACAP receptor expressed in freshly dispersed and cultured gastric and tenia coli smooth muscle cells of rabbit and guinea pig by reverse transcriptase-polymerase chain reaction (RT-PCR), Northern analysis, and cloning of the first extracellular domain. Specific primers based on cDNA sequences for rat VIP1/PACAP2, VIP2/PACAP3 and PACAP1 receptors were designed spanning the first extracellular domain. A 275 base pair product corresponding to VIP2/PACAP3 receptor was amplified by RT-PCR in muscle cells from both species. No RT-PCR product was obtained with primers for VIP1/PACAP2 and PACAP1 receptors. The deduced amino acid sequences showed 90% similarity in rabbit and 77% in guinea pig to the sequence in rat. The location of the aspartate, tryptophan and glycine residues and all six N-terminal cysteines required for VIP binding were conserved. The sequence in guinea pig tenia coli differed from that in guinea pig stomach by two amino acid residues, Phe40 and Phe41. Northern analysis revealed a single 3.9 kilobase (kb) mRNA corresponding to VIP2/PACAP3 receptors in rabbit and a 2.1 kb mRNA in guinea pig gastric and tenia coli muscle cells. We conclude that only VIP2/PACAP3 receptors are expressed in smooth muscle cells of rabbit and guinea pig. The two amino acid difference in the sequence obtained from guinea pig tenia coli may reflect the distinct binding and functional properties of this tissue.
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PMID:Selective expression of vasoactive intestinal peptide (VIP)2/pituitary adenylate cyclase-activating polypeptide (PACAP)3 receptors in rabbit and guinea pig gastric and tenia coli smooth muscle cells. 980 6