Substance P and opiate-like peptides in human adrenal medulla

Saria, Alois; Wilson, Steven P.; Molnar, A.; Viveros, O. Humberto; Lembeck, Fred

doi:10.1016/0304-3940(80)90145-7

Cited by 44 publications

(3 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bovine chromaffin granules contain, in addition to enkephalins, several other neuropeptides including substance P (Saria et al, 1980), neuropeptide Y (Waschek et al, 1987), galanin (Rokaeus et al, 1986), somatostatin (Lundberg et al, 1979), and endothelin (Sawamura et al, 1990) which are synthesized as precursors that require proteolytic processing.…”

mentioning

confidence: 99%

Purification and characterization of a cathepsin D protease from bovine chromaffin granules

Krieger¹,

Hook²

1992

Biochemistry

View full text Add to dashboard Cite

Purification and potential tachykinin and enkephalin precursor cleaving enzymes from bovine chromaffin granules was undertaken using as substrates the model precursors 35S-(Met)-beta-preprotachykinin [35S-(Met)-beta-PPT] and 35S-(Met)-preproenkephalin [35S-(Met)-PPE]. Purification by concanavalin A-Sepharose, Sephacryl S200, and chromatofocusing resulted in a chromaffin granule aspartyl protease (CGAP) that preferred the tachykinin over the enkephalin precursor. CGAP was composed of 47-, 30-, and 16.5-kDa polypeptides migrating as a single band in a nondenaturing electrophoretic gel system, and coeluting with an apparent molecular mass of 45-55 kDa by size-exclusion chromatography. These results suggest that two forms exist: a single 47-kDa polypeptide and a complex of 30 + 16.5-kDa-associated subunits. CGAP was optimally active at pH 5.0-5.5, indicating that it would be active within the acidic intragranular environment. Cleavage at basic residues was suggested by HPLC and HVE identification of 35S-(Met)-NKA-Gly-Lys as the major acid-soluble product generated from 35S-(Met)-beta-PPT. Neuropeptide K was cleaved at a Lys-Arg basic residue site, as determined by identification of proteolytic products by microsequencing and amino acid composition analyses. Structural studies showed that the three CGAP polypeptides were similar to bovine cathepsin D in NH2-terminal sequences and amino acid compositions, indicating that CGAP appears to be a cathepsin D-related protease or cathepsin D itself. The 47- and 16.5-kDa polypeptides of CGAP possessed identical NH2-terminal sequences, suggesting that the 16.5-kDa polypeptide may be derived from the 47-kDa form by proteolysis.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

mentioning

confidence: 99%

Purification and characterization of a cathepsin D protease from bovine chromaffin granules

Krieger¹,

Hook²

1992

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Over the past 30 years, adrenal medullary tissue has been used to obtain cultures of primary human chromaffin cells for developmental and functional studies with and without digestion before physical separation from the cortex (Tischler and Slayton 1983; Tischler et al 1985; Powers et al 1998, 2009; Cavadas et al 2001) and for therapeutic transplantation in multiple sclerosis (Lopez-Lozano et al 1989) and chronic pain patients (Lazorthes et al 1995; Sagen et al 1993). In some older publications, the identity of the collected cells was not verified (e.g., Saria et al 1980; Corder and Lowry 1982; Gaspar et al 1989). Other authors have verified chromaffin cell origin by testing the response to acetylcholine in vitro (Grazzini et al 1999), by measuring catecholamine levels (Evans et al 1983), by testing for TH immunoreactivity (Tischler and Slayton 1983; Tischler et al 1985; Powers et al 1998, 2009; Cavadas et al 2001; Lazorthes et al 1995; Bés et al 1998), or by labeling with neutral red and/or the catecholamine fluorescence technique (Hansen et al 1988; Crickard et al 1982; Lopez-Lozano et al 1989).…”

Section: Resultsmentioning

confidence: 99%

Tyrosine hydroxylase, chromogranin A, and steroidogenic acute regulator as markers for successful separation of human adrenal medulla

Fliedner¹,

Breza²,

Květňanský³

et al. 2010

Cell Tissue Res

View full text Add to dashboard Cite

Progress in high throughput “-omic” techniques now allows the simultaneous measurement of expression levels of thousands of genes and promises the improved understanding of the molecular biology of diseases such as cancer. Detection of the dysfunction of molecular pathways in diseases requires healthy control tissue. This is difficult to obtain from pheochromocytomas (PHEOs), rare chromaffin tumors derived from adrenal medulla. The two options for obtaining adrenal tissue are: (1) whole organ removal post-mortem or during radical nephrectomy; (2) removal during PHEO surgery. Access to high quality normal adrenal tissue is limited. Removal of whole adrenals during nephrectomy is rare, because of improved surgical techniques. For adrenals removed post-mortem, the lag time to proper organ perfusion causes uncontrolled tissue degradation. Adjacent normal adrenal tissue can almost never be obtained from resected PHEOs, because they often replace the entire medulla or are well-encapsulated. If a margin of normal adrenal is attached to a resected PHEO, it seldom contains any medulla. The clean separation of medulla and cortex is further complicated, because their border is convoluted, and because adult adrenal consists of ~90% cortex. Thus, the quality of separation has to be evaluated with specific medullary and cortical markers. We describe the successful dissection of highly pure, medullary tissue from adrenals snap-frozen upon resection during radical nephrectomy or after brain death. Separation quality has been verified by quantitative reverse transcription with polymerase chain reaction for the medullary enzymes, tyrosine hydroxylase, and chromogranin A, and for the cortical enzyme, steroidogenic acute regulator.

show abstract

“…In the adrenal medulla, SP functions to modulate the nicotinic secretion of catecholamines (Livett et al, 1990). SP-like immunoreactivity (SP-LI) has been detected in nerve terminals in the adrenal medulla (Saria et al, 1980;Bucsics et al, 198 I) and in cell bodies of sensory neurons in the dorsal root ganglia (DRG) that project to the adrenal medulla (Zhou et al, 1991). However, the chemical identity of this immunoreactive material (whether SP or another mammalian tachykinin) has yet to be determined.…”

mentioning

confidence: 99%

Chromatographic Evidence for the Presence of Multiple Tachykinins in the Bovine Adrenal Medulla

Basile

Cheung

Livett

1992

Journal of Neurochemistry

View full text Add to dashboard Cite

Among the mammalian tachykinins, substance P (SP) has been shown to be the most potent at modulating the response due to nicotinic acetylcholine receptor stimulation of bovine adrenal chromaffin cells. SP-like immunoreactivity has been detected in nerve terminals innervating the adrenal medulla; however, little is known of the presence of other tachykinins in this tissue. In this study, reverse-phase HPLC was used to fractionate peptides in bovine adrenal medullary extracts, and the fractions were analyzed by radioimmunoassay using antisera to SP or neurokinin A (NKA). The results show that both NKA- and SP-like immunoreactivities are present in the adrenal medulla. The presence of neurokinin B is also indicated. The presence of multiple tachykinins in this tissue raises questions as to their functions in the adrenal medulla.

show abstract

Substance P and opiate-like peptides in human adrenal medulla

Cited by 44 publications

References 16 publications

Purification and characterization of a cathepsin D protease from bovine chromaffin granules

Purification and characterization of a cathepsin D protease from bovine chromaffin granules

Tyrosine hydroxylase, chromogranin A, and steroidogenic acute regulator as markers for successful separation of human adrenal medulla

Chromatographic Evidence for the Presence of Multiple Tachykinins in the Bovine Adrenal Medulla

Contact Info

Product

Resources

About