Incidence peaks in melanoma and biopsy confirmed benign skin lesions--an effect of media campaigns?
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Biopsy↗
Biomedical subjects
P Pitkänen
Publications and source records attributed to P Pitkänen.
Indentation instrument for the measurement of cartilage stiffness under arthroscopic control.
Changes in the biomechanical properties of articular cartilage are one of the first signs of the tissue degeneration. We have developed a small size indentation instrument for the quantification of cartilage stiffness under arthroscopic control. During measurement, the indenter imposes a constant deformation on the cartilage and the maximal indenter force, by which the cartilage resists the deformation, is used as a measure for cartilage stiffness. The instrument has been tested in laboratory conditions with elastomer and cadaver knee joint cartilage samples. A linear relationship was found between indenter force and elastomer stiffness (r = 0.990, n = 14) as well as between indenter force and cartilage shear modulus obtained by a reference device (r = 0.879, n = 22). Also, the correlation between two repeated measurements at the measurement sites, used to evaluate the reproducibility, was linear (r = 0.953, n = 16). Quantitative detection of cartilage stiffness is possible with the instrument.
Arthroscopes↗
Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic polyneuropathy.
A prealbumin (PA)-like protein was demonstrated in amyloid fibrils both from a patient with senile systemic amyloidosis (SSA) and from a patient in northern Sweden with familial amyloidotic polyneuropathy (FAP). The investigated properties of this protein were similar in the two types of fibrils. The protein had molecular weight, antigenic determinants, and at least one cysteinyl residue in common with the subunit of normal PA. In contrast to normal PA, it contained disulphide-linked subunits and was to some extent bound to the fibril via the cysteinyl residues. The noncovalent forces between its subunits were weaker than in normal PA. It constituted part of the previously described AScl protein of the SSA fibrils. Proteins with lower molecular weight than the PA monomer were major proteins in both SSA and FAP fibrils. These proteins had similar properties in the two kinds of fibril and may be derived from PA. PA in serum from Swedish patients with FAP and SSA was normal with regard to the isoelectric pH of the monomers and tetramers.
Adult↗
Systemic amyloidosis: a review with emphasis on pathogenesis.
Our knowledge about the composition of the deposits in amyloidosis has increased considerably during the last decade. Three different protein groups have been shown to form fibrils in systemic amyloidosis, namely monoclonal immunoglobulin light chains in primary and myeloma-associated amyloidosis, protein AA in secondary amyloidosis and prealbumin in the familial and senile forms of systemic amyloidosis. This review deals with known and postulated pathogenetic mechanisms involved in the creation of fibrils from these proteins.
Aging↗
Serum prealbumin and retinol-binding protein in the prealbumin-related senile and familial forms of systemic amyloidosis.
In a series of 13 elderly patients with proven prealbumin-related senile systemic amyloidosis (SSA), depressed serum prealbumin values (110.7 +/- 14.1 micrograms/ml) were found as compared to an age-matched control group (175.1 +/- 20.3 micrograms/ml). As expected, there was a significant correlation between serum prealbumin and serum retinol-binding proteins in both groups of patients. Patients with reactive amyloid protein AA amyloidosis had slightly depressed serum prealbumin concentrations, whereas patients with prealbumin-related familial amyloidosis of Swedish type had prealbumin values within normal limits. Since the serum levels of the acute phase reactants, haptoglobin and amyloid-related serum protein AA, were higher in the group of patients with reactive amyloidosis than in patients with SSA, the depression of the prealbumin levels in SSA is not a result of inflammation. Since SSA is known to contain prealbumin, it is possible that a disturbed prealbumin metabolism in old age results in low prealbumin serum values and deposition of amyloid.
Adult↗
Histopathology of gastric carcinoids: a survey of 42 cases.
An unselected series of 42 gastric carcinoids has been reviewed. Clinically the tumours simulated common gastric lesions including ulcer, polyp and carcinoma. No endocrine symptoms were identified. The tumours were most frequent in the body of the stomach and in 25% in that site were multiple. Morphologically most tumours when classified according to Soga (1974) demonstrated a mixed growth pattern. Six tumours displayed an atypical morphology (type D): they were larger and metastasized more frequently than the rest of the tumours. Six tumours contained a few scattered argentaffinic cells but the others were negative indicating negligible serotonin secretion in only a few cases. The Grimelius argyrophilic reaction was positive in most cells in all tested tumours except in three, two of which showed atypical morphology (type D). It is suggested that gastric carcinoids with a type D morphology or a minority cell population of argyrophil cells are dedifferentiated carcinoids which are biologically nearer to gastric carcinomas. The most frequent clinicopathological correlation was achlorhydria linking pernicious anaemia and gastric carcinoids. This indicates pathogenetic similarities between gastric carcinoids and gastric carcinomas.
Adult↗
Senile systemic amyloidosis.
The senile amyloidoses comprise a heterogeneous group of disorders with deposition of amyloid in a variety of tissues. Most of these amyloidoses are localized to one tissue. It has been shown previously that the amyloid fibrils in one form of senile amyloidosis affecting the heart contains a prealbumin-related protein, ASc1. It is shown in this paper by immunohistochemical study using a specific anti-protein ASc1 antiserum that this type of amyloidosis, previously called senile cardiac amyloidosis, is a systemic disease with amyloid deposits in many organs. The designation senile systemic amyloidosis is proposed for this disease, which differs from other systemic amyloidoses in distribution of amyloid deposits.
Aged↗
Argyrophil endocrine cells with ACTH and HCG immunoreactivity in a carcinoma of the breast.
A middle-aged woman without any symptoms of ectopic hormone production underwent a right-sided mastectomy for infiltrating ductal carcinoma. She later developed axillary lymph node metastases which were somewhat carcinoid-like. This prompted further investigation, when scattered argyrophilic endocrine cells were found in both the primary tumour and its metastases. The endocrine cells reacted immunocytochemically with antisera against ACTH and HCG. Despite the endocrine activity of the tumour, it was still regarded as a ductal carcinoma since the endocrine cells constituted the minority cell population. The present study indicates strongly that ectopic hormone production in association with carcinoma of the breast is a result of hormone synthesis and release by the tumour cells.
Adrenocorticotropic Hormone↗
Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation.
Atrium, ventricle, aorta, lung, kidney, and rectum were removed at autopsy from 85 consecutive elderly patients (aged 80 years or older) and examined for amyloid with Congo red. All tissues containing amyloid were counterstained with an antiserum specific for amyloid fibril protein ASc1 and studied by immunofluorescence. Three distinct forms of amyloid were found: (1) all patients had senile aortic amyloid; (2) 78 percent of patients had isolated atrial amyloid; and (3) 25 percent of patients had senile cardiac amyloid of the ASc1 type. The cardiac amyloid deposits were small and widely scattered in more than 80 percent of patients with isolated atrial amyloid and in more than 50 percent of patients with ASc1-type amyloid. Of 21 patients with ASc1 amyloid, 19 had extracardiac involvement (lung in 81 percent of cases and rectum in 57 percent of cases). The kidney was not involved in any patient. The mean heart weight, frequency of atrial fibrillation, percentage of patients with heart failure, and frequency of myocardial infarction were increased in patients with cardiac amyloid, but these differences failed to reach statistical significance. There was no difference in the mean left ventricular wall thickness or degree of coronary atherosclerosis.
Aged↗
Amino acid sequences in amyloid proteins of kappa III immunoglobulin light-chain origin.
The main amyloid fibril (AL) proteins extracted from the spleen of Patient So 124 with systemic amyloidosis and from a skin nodule of Patient KSA with localized amyloidosis were studied by partial amino acid sequence analysis and proved to be of kappa III immunoglobulin light-chain origin. The sequences were similar to that of Bence Jones protein V and, which has been reported to have a unique kappa III subset sequence. Thus, except for position 9 in protein AL(KSA), the amino acid sequences were identical to position 25 in AL(So 124) and in AL(KSA). The question is being raised whether this kappa III subset might contain amyloidogenic sequences.
Aged↗
Right-sided hydrothorax complicating peritoneal dialysis. Report of 2 cases.
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Female↗
Amyloid of the seminal vesicles. A distinctive and common localized form of senile amyloidosis.
Amyloid deposits were found subepithelially in the seminal vesicles of 34 of 209 consecutively studied men. The incidence increased with age and was found in 21% of men over 75 years. This senile seminal vesicle amyloidosis (SSVA) is a localized disorder, and the amyloid substance has unique histochemical and immunochemical properties not shared with any other amyloid described until now.
Aged↗
Localized laryngeal amyloidosis: partial characterization of an amyloid fibril protein AL.
Amyloid fibrils were extracted from a patient Wr with more than 10 yr history of localized laryngeal amyloidosis. Degraded amyloid fibrils reacted in immunodiffusion with an antiserum against an amyloid protein of immunoglobulin kappa light chain origin, showing a line of identity with a kappa I amyloid protein. The protein Wr had a blocked aminoterminal, previously only reported in lambda chains. Amino acid sequence analysis of a fragment of the protein showed it to be an immunoglobulin light chain protein of V kappa I or V kappa III subgroup. The protein had a few unusual amino acid residues as compared to other kappa light chains. The findings support the view that the fibrils in localized, tumour-like amyloidosis are composed by homogeneous immunoglobulin light chain proteins in the same way as is seen in primary and myeloma associated systemic amyloidosis. It is possible that unusual light chains are over-represented in amyloid fibrils.
Amino Acid Sequence↗
Changes in the life expectancy of patients with severe haemophilia A in Finland in 1930-79.
Important advances have been made in the treatment of haemophilia during the past 30 years. We have analysed the data of all the known 163 patients with severe haemophilia A living in Finland in 1930-79 in order to study changes in the prognosis of severe haemophilia A. During the period of 50 years the mean age at death of the patients has increased from 7.8 years in 1930-39 to 25.5 years in 1970-79 and the annual death rate has markedly decreased in all age groups. The decline has been greatest in patients under 10 years of age. In this age group the annual death rate decreased from over 50 per thousand in 1930-39 and 1940-49 to 4.8 per thousand in 1970-79. The prognosis of patients with inhibitors has remained poor, however. Five of the six deaths during the last decade occurred in patients with inhibitors. The overall annual death rate of patients without inhibitors was only 1.2 per thousand in 1970-79, suggesting that at the present time the life expectancy of patients who do not develop inhibitors does not markedly differ from that of the general male population.
Adolescent↗
Senile aortic amyloid. A third distinctive type of age-related cardiovascular amyloid.
Aortic tissues from 22 elderly patients were analyzed by Congo red staining for amyloid deposits. All samples contained amyloid, which was resistant to the potassium permanganate reaction. Tryptophan was present in all amyloid deposits. The amyloid failed to react with antiserums to amyloid fibril protein ASc1 or human prealbumin, proteins previous demonstrated in generalized senile cardiac amyloid. It also differed from age-related isolated atrial amyloid, which has been shown to lack tryptophan. Deposits did not react with antiserums specific for amyloid fibril proteins of the A lambda IV, A lambda VI, AA, or AEt types. These results indicate that senile aortic amyloid is distinct from amyloid present in primary and secondary amyloidosis and appears to represent a third form of cardiovascular amyloid associated with the aging process.
Aged↗
[The treatment of hang-over].
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Alcoholic Intoxication↗