Isolation of Endogenous Hemorphin-Related Hemoglobin Fragments from Bovine Brain

Karelin, A. A.; Philippova, Marina M.; Karelina, E. V.; Иванов, В. Т.

doi:10.1006/bbrc.1994.1943

Cited by 68 publications

(37 citation statements)

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“…Since several hemorphins have been found in rive [3,9] and characterized by their biological properties [13,17], it will be of great interest to find out all the metabolic pathways from hemoglobin to hemorphins. Moreover, Carraway et al suggested the existence of a putative endogenous processing, similar to the renin-angiotensin system, which generates neurotensin-and enkephalin-related peptides in blood circulation [27,28].…”

Section: Resultsmentioning

confidence: 99%

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

Dagouassat¹,

Garreau²,

Sannier³

et al. 1996

FEBS Letters

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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.

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Section: Resultsmentioning

confidence: 99%

“…The same authors described the presence of LW-hemorphin-7 in cerebrospinal fluid (CSF) of patients with cerebrovascular bleeding [6], and hemorphin-7 in human plasma after long distance running [7,8]. Many other fragments of the beta-chain of hemoglobin have also been identified in rive [9].…”

Section: Introductionmentioning

confidence: 98%

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

Dagouassat¹,

Garreau²,

Sannier³

et al. 1996

FEBS Letters

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“…[12][13][14][15] At their targets the hemorphins could bind to the opioid receptor to mediate a wide spectra of biological functions such as analgesia, cardiovascular eŠect, gastrointestinal activity, behaviour, and eŠects on endocrine system. 16,17) We also hydrolysed hHb with leucocyte elastase and recovered traces of hemorphin-5 in the digest (data not shown).…”

Section: )mentioning

confidence: 99%

Release of Hemorphin-5 from Human Hemoglobin by Pancreatic Elastase

Jinsmaa

Yoshikawa

2002

Bioscience, Biotechnology, and Biochemistry

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“…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%

Bioactive angiotensin peptides

et al. 1998

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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...

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Isolation of Endogenous Hemorphin-Related Hemoglobin Fragments from Bovine Brain

Cited by 68 publications

References 0 publications

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

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

Release of Hemorphin-5 from Human Hemoglobin by Pancreatic Elastase

Bioactive angiotensin peptides

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