Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity

@article{Lantz1991HemorphinsDF,
  title={Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity},
  author={Ingrid Lantz and E L Gl{\"a}msta and L Talb{\"a}ck and Fred Nyberg},
  journal={FEBS Letters},
  year={1991},
  volume={287}
}

The hemorphins: a new class of opioid peptides derived from the blood protein hemoglobin.

This article will review recent studies of the hemorphins regarding their structures, mechanisms for their release, and their biological actions and place a particular emphasis on their role in exercising human and their clinical relevance.

Opioid peptides derived from hemoglobin: hemorphins.

Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors and the generation of VV-hemorphin-7 from globin by peritoneal macrophages.

Serum Hemorphin-7 Levels Are Decreased

Because obesity and type 2 diabetes share insulin resistance, high glomerular-filtration rate (GFR), microinflammation, and high cardiovascular risk, this work investigated whether obesity could also exhibit hemorphin abnormalities.

Primary structure and biological activity of hemoglobin-related hypothalamic peptides.

Five individual fractions from bovine hypothalamic extract, displaying coronary constrictory activity, were isolated and sequenced. All of them belong to the hemorphin group of hemoglobin-derived

Camel Hemorphins Exhibit a More Potent Angiotensin-I Converting Enzyme Inhibitory Activity than Other Mammalian Hemorphins: An In Silico and In Vitro Study

Angiotensin-I converting enzyme (ACE) is a zinc metallopeptidase that has an important role in regulating the renin-angiotensin-aldosterone system (RAAS). It is also an important drug target for the
...

References

SHOWING 1-10 OF 14 REFERENCES

A new class of angiotensin-converting enzyme inhibitors

This work reports on the design of a novel series of substituted N-carboxymethyl-dipeptides which are active in inhibiting angiotensin-converting enzyme at nanomolar levels and suggests that these compounds are transition-state inhibitors.

THE PREPARATION AND FUNCTION OF THE HYPERTENSIN-CONVERTING ENZYME

It has been shown by use of isolated, perfused rat kidneys that hypertensin II is a potent vasoconstrictor substance while hypertensin I is not. Hence it would appear that in intact animals the

Conversion of Angiotensin I to Angiotensin II

Results obtained with the blood bathed organ technique indicate that angiotensin I is converted rapidly to angiotensin II in the pulmonary circulation and not by an enzyme in the blood.

Fate of Angiotensin I in the Circulation

The results of the blood-bathed organ technique do not support hypotheses which suggest a completely intra-renal role for the renin–angiotensin system.

The Role of the Renin‐Angiotensin‐Aldosterone System in Cardiovascular Homeostasis in Normal Human Subjects

Results indicate that angiotensin II is essential for blood pressure maintenance in sodium depleted individuals, that angiotsin II exerts a direct feedback control on renin secretion, and that ang Elliotensin It is the primary stimulus to aldosterone secretion in response to both sodium depletion and to postur.