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We have cloned and characterized a second form of the human calcitonin receptor from T47D cells. It resembles the clone described by Gorn et al. [J. Clin. Invest. 90:1726-1735 (1992)] except that it lacks a 16-amino acid insert in the putative first intracellular loop. The insert-negative receptor appears to be the most abundant form, and it occurs at a relatively constant level in all expressing tissues. In contrast, the insert-positive receptor is found at low levels in most tissues but its expression levels appear to be much more variable. The insert-negative cDNA was stably expressed in baby hamster kidney cells. Like the endogenous T47D receptor, the recombinant receptor has an equally high affinity for salmon and porcine calcitonin but a 3-4-fold lower affinity for human calcitonin. High concentrations of calcitonin gene-related peptide, rat amylin, secretin, or vasoactive intestinal peptide do not significantly compete with calcitonin for binding to the recombinant receptor. Calcitonin stimulates a cAMP response in both T47D and transfected baby hamster kidney cells. Salmon calcitonin is more potent than human calcitonin for T47D cells, but the two are nearly equipotent for the transfectants. Furthermore, the ED50 for the cAMP response in the transfectants is 10-100-fold lower than in T47D cells. Calcitonin stimulates inositol phosphate turnover and elevates internal calcium levels in the transfectants. This response requires non-physiological levels of calcitonin and is directly correlated with the number of receptors. Lastly, by using a human/rodent somatic cell hybrid panel and in situ hybridization, we localized the human calcitonin receptor gene to chromosome 7.
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
November 1992,
The Journal of clinical investigation,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
April 1994,
The Journal of biological chemistry,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
September 1992,
Molecular pharmacology,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
December 1995,
Endocrinology,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
January 1991,
Transactions of the Association of American Physicians,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
December 1994,
Endocrinology,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
April 1998,
Endocrinology,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
February 2002,
Neuropeptides,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
May 1999,
Prostaglandins & other lipid mediators,
R E Kuestner, and
R D Elrod, and
F J Grant, and
F S Hagen, and
J L Kuijper, and
S L Matthewes, and
P J O'Hara, and
P O Sheppard, and
S D Stroop, and
D L Thompson
September 1997,
Molecular pharmacology,
