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Pakistanilawbooksinurdufreedownloadpdf _VERIFIED_

Pakistanilawbooksinurdufreedownloadpdf _VERIFIED_



 
 
 
 
 
 
 

Pakistanilawbooksinurdufreedownloadpdf

hope it’s helpfull:)

Characterization of the human parathyroid hormone and its receptor.
The identity of the second intracellular messenger for parathyroid hormone (PTH), cyclic adenosine monophosphate (cAMP) was investigated by using a variety of binding studies, including receptor autoradiography, pharmacology, and cross-competition with other agents, such as various cAMP-binding proteins. Competition studies with radiolabeled derivatives of cAMP, inositol-1,4,5-triphosphate (IP3), cyclic guanosine monophosphate (GMP), and cyclic guanosine tetraphosphate (GTP) revealed that the receptor for PTH resides in the cytoplasm. The binding potential of the receptor for cAMP (Kd, 10.4 nM; Bmax, 15.0 pmol/mg protein) was greater than that of the guanosine triphosphate (GTP)-binding protein (Kd, 104 nM; Bmax, 65 pmol/mg protein). The binding of [125I]PTH to the guanine nucleotide regulatory protein was inhibited by PTH in a concentration-dependent manner. When [125I]PTH binding to purified human renal basophilic cells was examined, a large proportion of the radioligand was bound with high affinity (Kd, 29 pM). The PTH receptor on guanine nucleotide regulatory protein in renal basophilic cells was found to exist in a high-affinity form that is activated by PTH. In contrast, low-affinity receptors in renal basophilic cells were found to be insensitive to PTH. The presence of a PTH receptor with high binding affinity (Kd, 29 pM) in renal basophilic cells was confirmed by using autoradiography with [125I]PTH. The present study demonstrated that PTH receptor on guanine nucleotide regulatory protein is mediated by cAMP. The present study also confirmed the presence of a class of high-affinity PTH receptors on renal basophilic cells. The functional significance of these two specific PTH receptors remains to be studied.

Affirmed and Opinion filed May 6, 2003

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