Plasma gut hormone levels in 37 patients with pheochromocytomas

Vinik, Aaron I.; Shapiro, Brahm; Thompson, Norman W.

doi:10.1007/bf01655534

Cited by 15 publications

(3 citation statements)

References 64 publications

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“…This expression is presumably in the adrenal medulla and is consistent with detection of MLIR in adrenal tissue (Yanihara, 1978) and with the report of elevated circulating motilin levels in a subset of patients with tumors of the adrenal medulla (Vinik et al, 1986). Motilin mRNA was also observed in the kidney.…”

Section: Discussionsupporting

confidence: 84%

Structure and Expression of the Human Motilin Gene

Daikh¹,

Douglass²,

Adelman³

1989

DNA

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The human motilin gene was isolated from a human genomic library and its structure was determined by restriction mapping and DNA sequence analysis. The gene consists of five exons separated by four introns spanning approximately 9 kb of genomic DNA. Exon I encodes the 5' untranslated portion of the motilin mRNA. Exons II and III encode the signal peptide and the 22-amino-acid motilin peptide; codons encoding the motilin moiety are split by an intron. The carboxy-terminal motilin-associated peptide (MAP) is largely encoded by Exons III and IV with the last two amino acids of the motilin precursor and the 3' untranslated region encoded by Exon V. Thus, the motilin gene has an unusual structure in which a small bioactive peptide is encoded on two distinct exons. Examination of the expression of the human and nonhuman primate motilin gene by Northern hybridization analysis indicates that it is expressed in a number of gastrointestinal and extragastrointestinal tissues.

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Section: Discussionsupporting

confidence: 84%

Structure and Expression of the Human Motilin Gene

Daikh¹,

Douglass²,

Adelman³

1989

DNA

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“…PC12 cells were found to show positive immunohistochemical staining with various motilin antisera; RIA of culture extracts confirmed these observations. A recent report documenting elevated plasma motilin levels in patients with pheochromocytomas (Vinik et al, 1986) provides additional evidence that these cells will be a n accurate model to study the nature of some of the motilin-reactivity in the rat. We plan to use this cell line to study motilin expression and regulation with cloned rat cDNAs.…”

Section: Cerebellummentioning

confidence: 97%

Heterogeneity of motilin immunoreactivity in mammalian tissue

Nilaver¹,

Beinfeld²,

Bond³

et al. 1988

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Motilin is a 22 amino acid peptide first isolated and sequenced from porcine gut. The use of antisera directed to the synthetic porcine gut motilin sequence has produced conflicting results as to regional distribution and histological localization of motilin in mammalian brain and gut. Motilin immunoreactivity has been detected (by RIA) in brain regions where no immunostaining is discernible. Variations in the patterns of staining are also observed with different antisera. These discrepancies have been explained by postulating species-, tissue-, and region-specific variations in peptide immunoreactivity, and variable cross reactivities of the independent antisera with these forms. The use of cloned porcine cDNA encoding gut prepromotilin in Northern blot analysis of brain regions expressing motilin-like immunoreactivity has also failed to reveal a homologous message, questioning the true nature of the immunoreactive material in the brain. Physiological studies, however, have suggested central roles for motilin in a variety of CNS (feeding behavior, bladder control, cerebral and brain stem modulation, pituitary growth hormone release) and gastrointestinal (gastric emptying, intestinal motility) functions. The motilin immunoreactive material detected in brain may be encoded by a distinct non-homologous gene, and still share amino acid homologies with the motilin sequence. Molecular biological characterization of the cell systems which contain motilin and motilin-like immunoreactivity should allow a better definition of their roles in these tissues.

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“…Variations in the occurrence and activation of such enzymes in the tumour cells could explain the aberrant de¬ grees of sulphation encountered here. Vinik et al (1986) showed that some pheochro¬ mocytomas secrete one or more of the hormones: somatostatin, motilin, substance and VIP to the blood, which could explain some of the great va¬ riety of symptons seen in these patients. There was no opportunity to measure plasma concentrations of CCK and gastrin in the present study, but as the gastrointestinal functions of CCK depend on tyrosine-O-sulphation (Ondetti et al 1970), dyspeptic symptoms owing to CCK overproduction would not be expected.…”

Section: Discussionmentioning

confidence: 98%

Cholecystokinin, gastrin and their precursors in pheochromocytomas

Bardram

Hilsted²,

Rehfeld³

1989

Acta Endocrinologica

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Using sequence-specific radioimmunoassays before and after cleavage with trypsin and carboxypeptidase B, we have examined the occurrence and molecular nature of cholecystokinin (CCK) and gastrin peptides in bioactive (i.e. \g=a\-carboxyamidated) as well as non-amidated precursor forms in extracts from 13 human pheochromocytomas. All but one tumour contained amidated CCK, but only in moderate amounts (\ m=l e\ 20 pmol/g tissue).In contrast to the complete sulphation in tissues which normally produce CCK (the brain and small intestine), the amidated adrenal CCK peptides were poorly sulphated (\ m=l e\17%). Four pheochromocytomas, including the one without amidated CCK, contained between 28 and 0.2 pmol amidated gastrin/g, mainly in the form of sulphated gastrin-17. In addition, all tumours contained biosynthetic precursors of both CCK and gastrin. In most extracts there was more precursor than bioactive peptide(s), the progastrin concentration ranging up to 338 pmol/g. The results show that pheochromocytomas synthesize CCK and gastrin. The posttranslational processing differs, however, markedly from that of the principal CCK and gastrin producing tissues, with respect to both proteolytic cleavages and amino acid derivatization. This emphasizes that accurate quantitation in tumours requires assays which measure the translation products irrespective of their degree of processing.

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Plasma gut hormone levels in 37 patients with pheochromocytomas

Cited by 15 publications

References 64 publications

Structure and Expression of the Human Motilin Gene

Structure and Expression of the Human Motilin Gene

Heterogeneity of motilin immunoreactivity in mammalian tissue

Cholecystokinin, gastrin and their precursors in pheochromocytomas

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