Isolation and characterization of a hemoglobin-derived opioid peptide from the human pituitary gland

Glämsta, Eva‐Lena; Marklund, Anna; Hellman, Ulf; Wernstedt, Christer; Terenius, Lars; Nyberg, Fred

doi:10.1016/0167-0115(91)90176-h

Cited by 106 publications

(63 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This peptide was called valorphin [4]. Another opioid peptide (LVV-hemorphin-6) was isolated from fresh frozen human pituitaries by Gliimsta et al [5]. Its primary *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Generation of VV‐hemorphin‐7 from globin by peritoneal macrophages

Dagouassat¹,

Garreau²,

Sannier³

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

Bovine globin has been incubated with mice peritoneal macrophages in order to study its hydrolysis by lysosomal enzymes, among which chiefly cathepsin D. Analysis of resulting peptides, by reversed-phase high-performance liquid chromatography (RP-HPLC), shown the release of a bioaetive peptide, VV-hemorphin-7. When a carboxyl proteinase inhibitor such as pepstatin A was added, no hemorphin was generated. Our results clearly demonstrated that VV-hemorphin-7 generation was principally due to cathepsin D. This study allowed us to hypothetize a possible pathway for in vivo hemorphins appearance from globin catabolism by macrophages.

show abstract

“…This peptide was called valorphin [4]. Another opioid peptide (LVV-hemorphin-6) was isolated from fresh frozen human pituitaries by Gliimsta et al [5]. Its primary *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Generation of VV‐hemorphin‐7 from globin by peritoneal macrophages

Dagouassat¹,

Garreau²,

Sannier³

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…85 This abundant peptide (approximately 2 nmol of peptide per gram of tissue) and Ang IV share very high affinity for the AT 4 receptor with their binding sites exhibiting very similar affinities for competing ligands and both peptides displayed very similar binding patterns. 85 The globin fragment has previously been isolated from different brain regions [86][87][88][89] and has been termed LVV-haemorphin-7. Furthermore, the enzymes pepsin, 90 trypsin 88 and a high molecular weight aspartic proteinase present in bovine brain, 91 are capable of cleaving the decapeptide from globin and is suggestive of processing in the central nervous system.…”

Section: Ang IVmentioning

confidence: 99%

“…85 The globin fragment has previously been isolated from different brain regions [86][87][88][89] and has been termed LVV-haemorphin-7. Furthermore, the enzymes pepsin, 90 trypsin 88 and a high molecular weight aspartic proteinase present in bovine brain, 91 are capable of cleaving the decapeptide from globin and is suggestive of processing in the central nervous system. Apart from inhibiting opioid activity, 90 our studies indicate that LVV-haemorphin-7 also inhibits neurite outgrowth from E11 chicken sympathetic neurons and stimulates DNA synthesis in neuronal cultures (unpublished observations).…”

Section: Ang IVmentioning

confidence: 99%

Bioactive angiotensin peptides

et al. 1998

View full text Add to dashboard Cite

Angiotensin II is recognised as the principle active peptide of the renin-angiotensin system, exerting effects on fluid and electrolyte homeostasis, and cardiovascular control including neural and long term trophic effects. However, recent studies indicate that other angiotensin peptides such as angiotensin III, angiotensin II (1-7) and angiotensin IV, may have specific actions. Interestingly, recent work involving angiotensin IV demonstrates that this peptide binds to specific receptors and may be Keywords: angiotensin metabolites; angiotensin III; angiotensin II(1-7); angiotensin IV; globin Bioactive angiotensin peptidesThe renin-angiotensin system (RAS) was initially identified as a circulating humoral system with the effector peptide, angiotensin II (Ang II), generated by an enzymatic cascade. Angiotensinogen, which is synthesized in the liver, is cleaved by renin, a product of the juxtaglomerular cells of the kidney, to form Ang I, which in turn is cleaved by angiotensinconverting enzyme (ACE) to form Ang II. ACE is membrane bound and predominates on the endothelial cells of all vascular beds. Apart from the production of Ang II in plasma, Ang II, renin and ACE have all been described in tissues such as the brain, kidney, adrenal, vasculature, heart and ovaries. This suggests a separate and distinct RAS in these tissues and implies endocrine, paracrine and autocrine roles for Ang II. Actions of Ang IIAng II regulates blood pressure, fluid volume homeostasis and pituitary hormone release via AT 1 and AT 2 receptors located in the kidney, adrenal gland, and the cardiovascular and nervous systems. [2][3][4][5] In the kidney, for instance, Ang II acts on renal vessels, glomeruli, tubules and renomedullary interstitial cells, to alter renal blood flow, glomerular filtration rate and electrolyte reabsorption.6-9 Ang II also acts on the adrenal cortex to stimulate aldosterone secretion and hence renal sodium reabsorption. 10Ang II is a potent vasoconstrictor, acting directly on vascular smooth muscle and indirectly via facilitation of noradrenaline release from sympathetic terminals. 11,12 In the heart, Ang II exerts positive iono- tropic and chronotropic effects and facilitates sympathetic activity. 13Acting on the brain, Ang II induces fluid and salt ingestion, modulates neuroendocrine systems, including vasopressin and corticotropin releasing factor release, and interacts with the autonomic control of the cardiovascular system to influence blood pressure. 3,14,15 In many instances, these effects are complementary to those of the systemic peptide on peripheral target organs. Thus, systematic Ang II affects the brain through AT 1 receptors located in the circumventricular organs, regions with a deficient blood brain barrier. In addition, endogenous neurally derived Ang II appears to act at many central nervous system sites behind the blood brain barrier. [16][17][18] Most of the classical actions of Ang II are mediated via the AT 1 receptor whereas AT 2 receptor stimulation may cause opposing effects. This was o...

show abstract

“…This peptide was orif~;nally isolated from the human pituitary gland [10]. The normal concentrations of this peptide in plasma has still not been determined or similarly its possible importance in blood pressure regulation.…”

Section: Introductionmentioning

confidence: 99%

“…The normal concentrations of this peptide in plasma has still not been determined or similarly its possible importance in blood pressure regulation. Apparently, LW-hemorphin-6 is a naturally occurring peptide which probably could be released from hemoglobin in the pituitary by the action of a trypsin-like and a chymotrypsin-like enzyme [10].…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of a bradykinin‐potentiating peptide from a bovine peptic hemoglobin hydrolysate

et al. 1992

View full text Add to dashboard Cite

A bradykinin potentiating ~ptide was isolated from a peptic bovine hemoglobin hydrolysate, by the use of reversed-phase high-performance liquid chromatography (RP-HPLC). Its primary structure, determined by fast atom bombardment (FAB) and tandem mass spectrometry (MS/MS), was identical to fragment 129-134 of the ~.chain of bovine hemoglobin. The bradykinin potency of this peptide, as exhibited by the guinea-pig ileum contraction, was significant and comparable with some others previously described.

show abstract

Isolation and characterization of a hemoglobin-derived opioid peptide from the human pituitary gland

Cited by 106 publications

References 18 publications

Generation of VV‐hemorphin‐7 from globin by peritoneal macrophages

Generation of VV‐hemorphin‐7 from globin by peritoneal macrophages

Bioactive angiotensin peptides

Isolation and characterization of a bradykinin‐potentiating peptide from a bovine peptic hemoglobin hydrolysate

Contact Info

Product

Resources

About