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Biomedical subjects

M Suda

Publications and source records attributed to M Suda.

At least 163 records · Page 9Linked to original sources
PubMed1985

Alpha-human atrial natriuretic polypeptide is released from the heart and circulates in the body.

In order to clarify whether or not atrial natriuretic polypeptides are hormones in man, we have measured plasma alpha-human atrial natriuretic polypeptide (alpha-hANP)-like immunoreactivity (alpha-hANP-LI) with or without extraction procedure. alpha-hANP-LI was detected in plasma extracts from all 5 normal subjects and 7 patients with heart diseases. The alpha-hANP-LI concentration in normal peripheral plasma was 37.7 +/- 7.0 pg/ml (mean +/- SE). Plasma concentrations of alpha-hANP-LI in the coronary sinus obtained by cardiac catheterization were 3 to 10 times higher than those in the peripheral vein, inferior vena cava, right atrium, pulmonary artery and aorta. High performance gel permeation chromatography coupled with a radioimmunoassay (RIA) for alpha-hANP revealed that alpha-hANP-LI in normal peripheral plasma eluted at the position corresponding to that of authentic alpha-hANP without detectable amounts of high molecular weight forms. alpha-hANP-LI extracted from plasma taken from the coronary sinus of two patients also showed a single peak of alpha-hANP-LI co-eluting with alpha-hANP. In contrast, not only alpha-hANP but gamma-hANP and beta-hANP, high molecular weight forms, were present in the human atrial tissue. These results indicate that alpha-hANP is the predominant form of alpha-hANP-LI in human plasma and that this form generated in the atrial cardiocytes is preferentially released from these cells and circulates in the body.

Adult↗
PubMed1985

Existence of atrial natriuretic polypeptide in kidney.

Using a specific radioimmunoassay (RIA) for alpha-atrial natriuretic polypeptide (alpha-ANP), we have demonstrated the presence of alpha-rat ANP-like immunoreactivity (alpha-rANP-LI) in the rat kidney which is considered to be a target organ for atrial natriuretic polypeptides released from the heart. Most of alpha-rANP-LI was localized in the cortex. High performance gel permeation chromatography coupled with the RIA revealed that renal alpha-rANP-LI was eluted at the position of a low molecular weight form corresponding to alpha-rANP without detectable amounts of high molecular weight forms. This is in contrast to the observation that gamma-rANP, a high molecular weight form of 13k daltons, is the dominant form of alpha-rANP-LI in the rat atrium. In water-deprived rats, the concentration and content of alpha-rANP-LI in the kidney showed a significant decrease compared with control rats. In addition, the alpha-rANP-LI concentration and content in this organ revealed a substantial decrease after perfusion with physiological saline. These results indicate the existence of atrial natriuretic polypeptide (ANP) in the kidney and suggest that part of renal ANP may originate from the heart.

Animals↗
PubMed1985

Occurrence of atrial natriuretic polypeptide in brain.

In order to determine whether or not atrial natriuretic polypeptides (ANPs) exist in the brain, we have studied extracts from the rat brain using a specific radioimmunoassay (RIA) for alpha-atrial natriuretic polypeptide. The presence and widespread distribution of alpha-rat ANP-like immunoreactivity (alpha-rANP-LI) have been demonstrated in the rat brain. The highest concentration of alpha-rANP-LI (20-22 ng/g) is in the hypothalamus and the septum. Moderate concentrations of alpha-rANP-LI (2-8 ng/g) are also found in the midbrain, cerebral cortex, olfactory bulb, thalamus, pons-medulla and hippocampus. High performance gel permeation chromatography coupled with the RIA revealed that alpha-rANP-LI found in the rat brain consists of three components eluting at the positions of gamma-rat ANP (gamma-rANP), beta-rat ANP (beta-rANP) and alpha-rANP, respectively. Among these a low molecular weight form of alpha-rANP-LI emerging at the elution position corresponding to alpha-rANP is predominant in the rat brain. This is in contrast to the finding that gamma-rANP, a high molecular weight form of 13k daltons is the dominant form of alpha-rANP-LI in the rat atrium. These results clearly show that there exists a widespread neural system containing ANPs in the brain.

Animals↗
PubMed1985

Leumorphin in human brain.

Porcine leumorphin, a putative opioid peptide corresponding to amino acid residues 228-256 of preproenkephalin B has been demonstrated to exist in the porcine neurointermediate pituitary. A recent study on the sequence analysis of genomic DNA of human preproenkephalin B has shown that human leumorphin differs in 3 amino acid residues from porcine leumorphin. In order to clarify whether leumorphin is an endogenous opioid peptide in man, we have studied its existence and regional distribution in the human brain using a radioimmunoassay (RIA) for leumorphin. Reverse-phase HPLC and high performance gel permeation chromatography coupled with the RIA for leumorphin revealed that human leumorphin existed together with rimorphin (dynorphin B) in water extracts of the human brain. Leumorphin-like immunoreactivity (-LI) and dynorphin-LI distributed in parallel throughout the brain. These results indicate that leumorphin is a novel endogenous opioid peptide in man.

Animals↗
PubMed1985

Endogenous opioids and related peptides: from molecular biology to clinical medicine. The Sir Henry Dale lecture for 1985.

Advances in techniques in molecular biology have facilitated the research into endogenous opioids and related peptides in several ways. The organization and expression of genes and the primary structure of three precursor proteins of opioid peptides have been elucidated. These studies predicted the presence of potentially bioactive peptides, which has been confirmed by later studies. Advances in techniques in protein chemistry have helped to elucidate the distribution and molecular forms of endogenous opioids and related peptides in the body, and the processing of precursor proteins. Studies on the function of these peptides have shown a broad spectrum of actions. Leumorphin, a newly identified peptide, has been shown to exhibit unique biological activities. In spite of extensive studies, the physiological and pathophysiological significance of opioid peptide systems are not yet completely understood. This is mainly due to the paucity of our knowledge about opioid receptors. Further studies on the subtypes of opioid receptors will help to elucidate all aspects of the function of endogenous opioids and related peptides.

Animals↗
PubMed1985

Accelerated natriuresis induced by synthetic atrial natriuretic polypeptide in spontaneously hypertensive rats.

Effects of synthetic alpha human atrial natriuretic polypeptide (alpha-hANP) on diuresis, natriuresis and mean arterial blood pressure (MAP) were compared between 4-5 month-old male spontaneously hypertensive rats (SHR) and Wistar-Kyoto rats (WKY) under ether anesthesia. In both groups, the peptide injected (0.5 micrograms/100g body weight, i.v.) caused potent (about ten fold), rapid and short-acting (for 15 min) increases in sodium (Na+) and chloride excretions and also an increase in urine flow and potassium excretion with lesser magnitude. Although ratios of the maximum response to basal value were much the same, net increases in urine flow and Na+ output were significantly greater in SHR than in WKY. As to the effect on MAP, a rapid (within 2 min) fall observed in the two groups. These results suggest that the atrial natriuretic peptide may be involved in the altered regulatory mechanism of fluid and electrolyte balance in SHR models with genetic hypertension.

Animals↗
PubMed1984

Radioimmunoassay for alpha-human and rat atrial natriuretic polypeptide.

Using a synthetic common carboxy-terminal fragment of alpha-human atrial natriuretic polypeptide (alpha-hANP) and alpha-rat atrial natriuretic polypeptide (alpha-rANP), we have produced an antiserum for alpha-ANP(17-28) and established a radioimmunoassay (RIA) for alpha-ANP that recognizes alpha-hANP and alpha-rANP equally. High performance gel permeation chromatography coupled with the RIA revealed that alpha-hANP-like immunoreactivity (alpha-hANP-LI) in the human atrium consists of three major components, gamma-hANP, alpha-hANP and another. On the other hand, alpha-rANP-LI in the rat atrium comprised at least two components, 13K alpha-rANP-LI and 3K-5K alpha-rANP-LI, which were presumably gamma-rANP and beta-rANP, respectively. Thus, considerable amounts of gamma-hANP and gamma-rANP are present in human right auricles and rat atria, respectively. The RIA established in this study provides a useful tool to investigate the pathophysiological significance of alpha-ANP and related peptides in cardiovascular disorders and shows that gamma-ANP is not only a precursor of alpha-ANP but acts as an important hormone.

Amino Acid Sequence↗
PubMed1984

Human leumorphin is a potent, kappa opioid receptor agonist.

The opioid activity and opioid receptor type specificity of synthetic human leumorphin were studied in vitro. Human leumorphin inhibited the contraction of the myenteric plexus-longitudinal muscle preparation of the guinea pig ileum and was similar in opioid potency to porcine leumorphin. This action of human leumorphin was antagonized less effectively by naloxone than by the opiate antagonist Mr 2266. Human leumorphin also inhibited the contraction of the rabbit vas deferens which has only the kappa-type opioid receptor. It is concluded that human leumorphin has potent opioid activity and acts as an agonist at the kappa-type opioid receptor, like porcine leumorphin and other peptides derived from preproenkephalin B.

Animals↗
PubMed1984

Leumorphin is a novel endogenous opioid peptide in man.

Porcine leumorphin, a putative opioid peptide corresponding to amino acid residues 228-256 of preproenkephalin B has been demonstrated to exist in the porcine neurointermediate pituitary. A recent study on the sequence analysis of genomic DNA of human preproenkephalin B has shown that human leumorphin differs in 3 amino acid residues from porcine leumorphin. In order to clarify whether leumorphin is an endogenous opioid peptide in man, we have studied its existence in the human brain using a radioimmunoassay and its opioid activity by a bioassay with the guinea-pig ileum myenteric plexus-longitudinal muscle preparation. High performance gel permeation chromatography and reverse-phase high performance liquid chromatography coupled with the radioimmunoassay for leumorphin have revealed that human leumorphin exists in water extracts of the human striatum. In the guinea-pig ileum assay, synthetic human leumorphin exhibited potent opioid activity, with the concentration of 3nM to give 50 per cent inhibition. These results indicate that leumorphin is a novel endogenous opioid peptide in man.

Adult↗
PubMed1984

Analysis of cerebellar motor disorders by visually guided elbow tracking movement.

Motor control was analysed by a visuomotor tracking movement using elbow flexion both in patients with cerebellar ataxia and in normal controls. A TV screen was divided into upper and lower halves, in each of which a vertical strip was displayed. The upper strip (T, target) was moved horizontally from the centre of the screen to the left or right by ramp voltage. The lower strip (D, displacement of the handle) was moved in proportion to angular displacement of the handle by a potentiometer coupled to the handle axis. The subject, while sitting in front of the TV screen, had to make D match the movement of T by controlling the handle with his right arm. The range of T movement was 30 deg in terms of the handle's angular movement. T velocity was 7.5, 15 or 30 deg/s. The subjects were told the direction and velocity of T in advance. The process of tracking was divided into three phases (initial catch-up phase, middle pursuit phase, and terminal phase), in each of which the performance of cerebellar ataxia patients differed from that of the controls. The characteristic features of the ataxic cases were (1) prolongation of the reaction time, mainly due to the increase of premotor time; (2) difficulty in selecting an appropriate amplitude of initial peak velocity in proportion to the target velocity in the initial catch-up phase; (3) disruption of smooth continuous movement, namely, the saccadic pattern in the middle pursuit phase; (4) delay in the initiation of deceleration in the terminal phase; (5) difficulty in corrective adjustment in reaching the final target point; and (6) irregular EMG activity in the agonist muscles and/or cocontraction of the antagonistic muscles. Quantitative treatment of the second and third features, as exemplified in the relationship between initial error and initial peak velocity and in the ratio of the movement arrest period, respectively, was found to be helpful in the evaluation of disease severity. The significance of these findings is discussed and the role of the cerebellar system in the control of slow voluntary movement is stressed.

Adult↗
PubMed1984

Demonstration and characterization of immunoreactive methionine-enkephalin, leucine-enkephalin, methionine-enkephalin-Arg6-Gly7-Leu8 and methionine-enkephalin-Arg6-Phe7 in human phaeochromocytoma.

To elucidate whether or not human phaeochromocytoma contains methionine-enkephalin-Arg6-Gly7-Leu8 (Met-enkephalin-Arg-Gly-Leu) and methionine-enkephalin-Arg6-Phe7 (Met-enkephalin-Arg-Phe) together with methionine-enkephalin (Met-enkephalin) and leucine-enkephalin (Leu-enkephalin), all of which are known to exist in the same precursor molecule (preproenkephalin A), we examined extracts from 16 phaeochromocytomas using high performance liquid chromatography (HPLC) and gel exclusion chromatography coupled with radioimmunoassays (RIAs) for these four opioid peptides. Met-enkephalin-Arg-Gly-Leu-like immunoreactivity (-LI) and Met-enkephalin-Arg-Phe-LI existed together with Met-enkephalin-LI and Leu-enkephalin-LI in 16 phaeochromocytomas. There was a wide variation in contents of Met-enkephalin-LI, Leu-enkephalin-LI, Met-enkephalin-Arg-Gly-Leu-LI and Met-enkephalin-Arg-Phe-LI. Significant positive correlations were observed among the contents of these four opioid peptides in 16 phaeochromocytomas. HPLC and gel exclusion chromatography followed by the RIAs showed the presence of Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Gly-Leu and Met-enkephalin-Arg-Phe together with their high molecular weight forms, which existed in variable amounts. Molar ratios of the contents of these four opioid peptides determined after HPLC varies from case to case. These results indicate the co-existence of Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Gly-Leu and Met-enkephalin-Arg-Phe in human phaeochromocytomas, suggesting the preservation of amino acid sequences of these four opioid peptides even in neoplastic tissues.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1983

Leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B.

Using synthetic leumorphin, we obtained antisera for leumorphin and set up two radioimmunoassays (RIAs) with different specificities. Gel exclusion chromatography coupled with the two RIAs showed the existence of a considerable amount of leumorphin-like peptide in water extracts from porcine neuro-intermediate pituitaries. Reverse phase high performance liquid chromatography revealed that leumorphin-like peptide in the water extracts was indistinguishable from synthetic leumorphin. These results along with potent opioid activity of leumorphin indicate that leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B.

Animals↗
PubMed1983

A novel opioid peptide, leumorphin, acts as an agonist at the kappa opiate receptor.

The primary structure of the common precursor of porcine beta-neo-endorphin and dynorphin (preproenkephalin B) has shown the existence of a third leucine-enkephalin (leu-enkephalin) sequence with a C-terminal extension of 24 amino acids. This nonacosapeptide, named leumorphin, was approximately 70 times more potent than leu-enkephalin in inhibiting the contraction of the myenteric plexus-longitudinal muscle preparation of the guinea pig ileum. This action of leumorphin, like those of beta-neo-endorphin and dynorphin, was antagonized less effectively by naloxone than that of leu-enkephalin, but more effectively by Mr2266, an antagonist relatively specific for the kappa type opiate receptor. The inhibitory action of leumorphin or beta-neo-endorphin on the contraction of the guinea pig ileum muscle strip was reduced in a dose-dependent manner by pretreatment with dynorphin and vice versa. Leumorphin as well as beta-neo-endorphin and dynorphin inhibits the contraction of the rabbit vas deferens which is known to have only the kappa type opiate receptor. This action was also effectively antagonized by Mr2266. It is concluded that leumorphin has potent opioid activity and acts at the kappa receptor, like other opioid peptides derived from preproenkephalin B.

Animals↗
PubMed1983

Rimorphin (dynorphin B) exists together with alpha-neo-endorphin and dynorphin (dynorphin A) in human hypothalamus.

Rimorphin (dynorphin B) has been demonstrated to exist together with alpha-neo-endorphin and dynorphin(1-17) (dynorphin A) in the human hypothalamus. The content of rimorphin was comparable to that of alpha-neo-endorphin and somewhat higher than that of dynorphin. This result is quite similar to the recent observations in bovine, porcine and rat neural tissues, suggesting that rimorphin is derived from preproenkephal in B together with alpha-neo-endorphin and dynorphin in man.

Adult↗
PubMed1983

Biosynthesis and distribution of opioid peptides.

Group III opioid peptides are derived from proenkephalin B. The processing of this precursor peptide is still only partly understood and we still do not know how many final products come from proenkephalin B and whether Leu-enkephalin is produced from Group III peptides. However, potent biologic activity of Group III opioid peptides and existence of opiate-receptors specific for these peptides (k receptors) strongly suggest that Group III opioid peptides are not precursors of Leu-enkephalin but bioactive substances per se. Further studies should clarify details of the processing of proenkephalin B.

Adrenal Medulla↗