Showing papers by "Rosalyn S. Yalow published in 1975"
TL;DR: This hypothesis is strengthened by the observation that all stages of acute pancreatitis have been produced in dogs by incomplete obstruction of the pancreatic duct, and the general concept that increased intraductal pressure, caused by secretion against obstruction, may produce disruption of pancreatic radicals and escape of enzymes into the tissues, thereby causing pancreatic damage.
Abstract: MANY pathophysiologic mechanisms have been proposed to explain the role of alcohol in the development of acute pancreatitis in the almost 100 years since "drunkard's pancreas" was first described.1 At present no mechanism has been proved. However a great deal of attention has been paid to the general concept that increased intraductal pressure, caused by secretion against obstruction, may produce disruption of pancreatic radicals and escape of enzymes into the tissues, thereby causing pancreatic damage.2 This hypothesis is strengthened by the observation that all stages of acute pancreatitis have been produced in dogs by incomplete obstruction of the pancreatic duct . . .
58 citations
TL;DR: The observation that blood concentrations in terms of porcine gastrin standard are comparable to those of pig, man, and dog suggests significant homology between the structures of molluscan and mammalian gastrins.
Abstract: Blood and gastrointestinal tissues of the sea hare Aplysia californica and the land snail Otala lactea contain immunoreactive gastrin in heterogeneous forms similar to those of mammals. The observation that blood concentrations in terms of porcine gastrin standard are comparable to those of pig, man, and dog suggests significant homology between the structures of molluscan and mammalian gastrins.
47 citations
TL;DR: A radioimmunoassay has been developed for Somatomedin B, a growth hormone-dependent factor that stimulates DNA synthesis in human glia-like cells that is found predominantly in Cohn plasma fractions III and IV, largely dissociated from the plasma-binding protein.
Abstract: A radioimmunoassay has been developed for Somatomedin B, a growth hormone-dependent factor that stimulates DNA synthesis in human glia-like cells. The sensitivity permits detection of this factor in human plasma diluted 1: 20,000 and in monkey plasma diluted 1: 5,000. It is not measurable in nonprimate plasma diluted 1: 20. The concentration in growth hormone-deficient adult patients is equivalent to 6.6plus or minus0.5 ug/ml of a highly purified somatomedin preparation. In acromegaly the concentration is 19.3plus or minus2.3 ug/ml and falls after definitive therapy that results in a decrease in plasma growth hormone. In unextracted human plasma the immunoreactive Somatomedin B is associated with a plasma protein at least as large as gamma-globulin and with an electrophoretic mobility on paper resembling the alpha-globulins. The level of Somatomedin B in the bound form in human plasma under steady-state conditions may depend on the rate of production of the peptide and/or the concentration of the plasma-binding protein. At present there is no information concerning which of these is modulated by growth hormone. Immunoreactive Somatomedin B is found predominantly in Cohn plasma fractions III and IV, largely dissociated from the plasma-binding protein. The disappearance curves of labeled purified Somatomedin B and of immunoreactive Somatomedin B from acromegalic plasma administered intravenously to a dog were superposable; the terminal portion of the disappearance curve having a half time of almost an hour.
34 citations
TL;DR: The potential usefulness of adrenocorticotropic hormone (ACTH) determinations in diagnosis and in prognosis for therapy of patients with carcinoma of the lung but without clinical Cushing's syndrome is considered.
Abstract: This report considers the potential usefulness of adrenocorticotropic hormone (ACTH) determinations in diagnosis and in prognosis for therapy of patients with carcinoma of the lung but without clinical Cushing's syndrome. The report is based on radioimmunoassay data from 129 patients, including 62 with lung cancers and 67 with nonmalignant pulmonary conditions. Elevated plasma ACTH was found in 21 of 24 patients with untreated cancer and the hormone was detected in tumor extracts and/or bronchial washings from the remaining 3. Elevation of plasma ACTH was found in only 10 of 38 treated patients. Absence of clinical Cushing's syndrome in spite of high plasma ACTH concentrations is explained by the observation that the predominant form of ectopic ACTH in plasma is immunoreactive but nonbioactive 'big' ACTH. Prolonged survival, for longer than 19 months, was observed in only 5 patients: all patients with low plasma ACTH after resection of the lung tumor and 2 of 3 patients with low plasma ACTH without therapy. ACTH was found in all available malignant tissue, primary and metastatic, from the lung carcinoma group,but not in normal lung or in 5 tumors metastatic to the lung. Of the 39 patients diagnosed initially to have chronic obstructive pulmonary disease, 14 showed plasma ACTH elevation. However, 3 of these patients with the highest concentrations subsequently manifested carcinoma or carcinoma in situ.
32 citations
TL;DR: Control tryptic digestion of mouse-tumor big ACTH results within 10 seconds in conversion to an intermediate component followed by continued loss of immunoreactivity, which strengthens the hypothesis that mouse intermediate ACTH is not a precursor for little ACTH.
Abstract: The predominant component of immunoreactive ACTH in the plasma of adrenalectomized normal mice and of mice bearing the adrenotropic mouse pituitary tumor, AtT-20, and in extracts of the normal mouse pituitary and pituitary tumor, has an elution volume on Sephadex G-50 gel filtration approximately midway between the void volume and the elution volume of human ACTH (1-39 peptide). The tumor extracts are shown to contain, in addition to this intermediate ACTH, 2 other components of immunoreactive ACTH, one which coelutes with 131I-labeled albumin (big ACTH) and the other with [125I]hACTH (little ACTH). Big and intermediate ACTH are urea-stable. Controlled tryptic digestion of mouse-tumor big ACTH results within 10 seconds in conversion to an intermediate component followed by continued loss of immunoreactivity. Under the same conditions of tryptic digestion of intermediate ACTH, there is only continuous loss of immuno-reactivity with no change of hormonal form. These findings strengthen the hypothesis that mouse intermediate ACTH is not a precursor for little ACTH.
26 citations
TL;DR: It is found that although the rate of iodination of 6-Tyr-secretin is more rapid than that of secretin, the efficiency of iodinations is not greatly increased and the shelf-life of the labeled product is not prolonged.
20 citations
TL;DR: The level of somatomedin B in the bound form in human plasma under steady-state conditions may depend on the rate of production of the peptide and/or the concentration of the plasma binding protein.
Abstract: Publisher Summary This chapter provides an overview of radioimmunoassay of somatomedin B. The sensitivity of the assay permits the measurement of this factor in human plasma diluted 1:20,000 and in monkey plasma diluted 1:5000. Somatomedin B is not detected in many nonprimate plasmas diluted 1:20. In this regard, the species specificity of the radioimmunoassay resembles that of hGH. In unextracted human plasma, the immunoreactive somatomedin B is associated with a plasma protein, which is at least as large as γ-globulin and has an electrophoretic mobility on paper resembling that of the α-globulins. That the binding to plasma protein is noncovalent is indicated by the ready adsorption of endogenous somatomedin B to charcoal in diluted plasma as well as by the rapid disappearance of immunoreactive somatomedin B from the circulation of a dog following administration of human plasma somatomedin B. The level of somatomedin B in the bound form in human plasma under steady-state conditions may depend on the rate of production of the peptide and/or the concentration of the plasma binding protein.
9 citations
TL;DR: Urinary excretion by 8 normal adult subjects of immunoreactive somatomedin B was 27.6 +/- 4.4 mug between 1000 h and 1400 h compared to a mean plasma concentration at 1200 h of 5.9 +/- 0.9 mug/ml, although in the plasma of the same subjects all but less than 5% was bound to serum proteins.
Abstract: Urinary excretion by 8 normal adult subjects of immunoreactive somatomedin B was 27.6 ± 4.4 μg between 1000 h and 1400 h compared to a mean plasma concentration at 1200 h of 5.9 ± 0.9 μg/ml. Free somatomedin B in urine averaged 85.9%, although in the plasma of the same subjects all but less than 5% was bound to serum proteins.
6 citations