PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “PAM”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 415 records · Page 23Linked to original sources
PubMed1995

Endogenous porphyrins in murine skin and transplanted PAM-212 squamous cell carcinoma tissues after injection of delta-aminolevulinic acid.

After intraperitoneal (IP) injection of delta-aminolevulinic acid (ALA), the endogenous porphyrins in murine skin and tumor tissues were determined by a method involving solvent and acid extractions. The results showed that the total amount of porphyrins in the tumor tissues after ALA injection was much higher than that in the skin from the same mice, although the amount of porphyrins in the skin from the ALA-injected mice was higher than that from the saline-injected (control) mice. The porphyrins in the tumor were mostly protoporphyrin and coproporphyrin, with only a small amount of uroporphyrin. The optimum period for porphyrin accumulation in the tumor as well as in the skin was 1 hour after the injection of ALA. As the period was extended to 3 and 6 hours, the amount of porphyrins in these tissues decreased considerably. These findings could be valuable for further application of ALA in the photodynamic therapy of skin cancer.

Aminolevulinic Acid↗
PubMed1993

[Ovarian neoplasms in children taken from material of the pediatric children's clinic PAM in Szczecin].

The authors analysed 19 girls aged six to fourteen years with tumors of ovary treated in the last 27 years in the Department of Pediatric Surgery, Pomeranian Medical Academy in Szczecin. Symptoms procedures tactics, advantage of neoplastic markers in diagnosis and treatment monitoring of malignant processes are discussed. The authors warned against to hastily and to spare operations instead of adnexectomy. This procedure is recognized by many as a typical for girls with ovary tumors.

Adolescent↗
PubMed1996

Expression of peptidyl-glycine alpha-amidating mono-oxygenase (PAM) enzymes in morphological abnormalities adjacent to pulmonary tumors.

Carboxyl-terminal amidated peptide hormones are known to be autocrine growth factors for lung tumors and tumor cell lines. Expression of the enzymes necessary for the biosynthesis of active amidated peptide hormones is therefore necessary for autocrine growth stimulation in lung tumors and possibly in the early proliferative stages of lung carcinogenesis. The peptidyl amidating enzymes have previously been identified in cell lines of all histological types of lung cancer and in lung tumors by immunohistochemistry and in situ hybridization. In this study we analyzed the expression of the peptidyl amidating enzymes in histological abnormalities found in the proximity of pulmonary tumors from a series of 59 patients. Most of the lesions in both the proximal airways (basal cell hyperplasia, carcinoma in situ, and some squamous metaplasia) and the alveoli (type II cell hyperplasia, bronchiolization of the alveoli, atypical alveolar hyperplasia, and isolated atypias) had a high proportion of cells strongly positive for the peptidyl amidating enzymes. The intense expression of peptidyl amidating enzymes in type II cell hyperplasia and atypical alveolar cells, together with the high frequency of these abnormalities in the alveoli, which is an area that does not express these enzymes in normal lung, points to the involvement of peptide hormones in the growth biology of pulmonary tumors. These findings suggest that peptide hormone stimulation of mitogenesis is an early event in tumor progression and merits additional investigation as a target for early detection and chemo-intervention of lung carcinogenesis.

Adult↗
PubMed1996

[Bacterial flora of acne lesions in diagnostic material of the Microbiology and Immunology Department, Pomeranian Medical Academy (PAM) in Szczecin].

A retrospective analysis of the bacterial flora of acne lesions was carried out in 320 patients. Atypical flora was isolated very rarely. The pathogenic flora was found most frequently in the Autovaccine Laboratory when the microbiological material was taken directly onto plates and the investigation was repeated several times. Atypical flora was isolated only from three cases. Propionibacterium and Staphylococcus epidermidis were found to be sensitive to the antibiotics routinely used in the treatment of acne. The highest antibacterial effect in vitro against both these species was demonstrated using rifampicin and tetracycline.

Acne Vulgaris↗
PubMed2002

Polyacrylamide preparations for protection of water quality threatened by agricultural runoff contaminants.

Waste streams associated with a variety of agricultural runoff sources are major contributors of nutrients, pesticides and enteric microorganisms to surface and ground waters. Water soluble anionic polyacrylamide (PAM) was found to be a highly effective erosion-preventing and infiltration-enhancing polymer, when applied at rates of 1-10 g m(-3) in furrow irrigation water. Water flowing from PAM treated irrigation furrows show large reductions in sediment, nutrients and pesticides. Recently PAM and PAM + CaO and PAM + Al(SO4)3 mixtures have been shown to filter bacteria, fungi and nutrients from animal wastewater. Low concentrations of PAM [175-350 g PAM ha(-1) as PAM or as PAM + CaO and PAM + Al(SO4) mixture] applied to the soil surface, resulted in dramatic decreases (10 fold) of total, coliform and fecal streptococci bacteria in cattle, fish and swine wastewater leachate and surface runoff. PAM treatment also filtered significant amounts of NH4, PO4 and total P in cattle and swine wastewater. This points to the potential of developing PAM as a water quality protection measure in combination with large-scale animal feeding operations. Potential benefits of PAM treatment of animal facility waste streams include: (1) low cost, (2) easy and quick application. (3) suitability for use with other pollution reduction techniques. Research on the efficacy of PAM for removal of protozoan parasites and viruses and more thorough assessment of PAM degradation in different soils is still needed to completely evaluate PAM treatment as an effective waste water treatment. We will present analysis and feasibility of using PAM, PAM + Al(SO4)3, and PAM + CaO application for specific applications. Our results demonstrate their potential efficacy in reducing sediment, nutrients and microorganisms from animal production facility effluents.

Acrylic Resins↗
PubMed1993

COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells.

Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the COOH-terminal amidation of bioactive peptides through a two step reaction catalyzed by separate enzymes contained within the PAM precursor. To characterize the trafficking of integral membrane PAM proteins in neuroendocrine cells, we have generated stable AtT-20 cell lines expressing full length and COOH-terminally truncated integral membrane PAM proteins. Full length integral membrane PAM was present on the cell surface in low but detectable amounts and PAM proteins which reached the cell surface were rapidly internalized but not immediately degraded in lysosomes. Internalized PAM complexed with PAM antibody was found in a subcellular compartment which overlapped with internalized transferrin and with structures binding WGA. Thus the punctate juxtanuclear staining of full length PAM represents PAM in endosomes. Endoproteolytic processing of full length PAM-1 and PAM-2 resulted in the secretion of soluble PAM proteins; the secretion of these soluble PAM proteins was stimulus dependent. Although some of the truncated PAM protein was also processed and stored in AtT-20 cells, much of the expressed protein was redistributed to the plasma membrane. Soluble proteins not observed in large amounts in cells expressing full length PAM were released from the surface of cells expressing truncated PAM and little internalization of truncated integral membrane PAM was observed. Thus, the COOH-terminal domain of PAM contains information important for its trafficking within the regulated secretory pathway as well as information necessary for its retrieval from the cell surface.

Animals↗
PubMed1993

Maturation, internalization, and turnover of soluble and membrane proteins associated with atrial myocyte secretory granules.

Primary cultures of neonatal atrial myocytes were used to study the biosynthesis of a prominent secretory granule enzyme that occurs naturally in soluble and integral membrane forms. The two most prominent forms of peptidylglycine alpha-amidating monooxygenase PAM) in atrial myocytes are type I integral membrane proteins (PAM-1 and -2); smaller amounts of a soluble form, PAM-3, are also found. All three PAM proteins are N-glycosylated, and PAM-1 also has sialylated O-linked oligosaccharide. Two hours after their biosynthesis, approximately half of the newly synthesized PAM-1 and PAM-2 proteins have acquired N-linked oligosaccharide chains resistant to digestion with endoglycosidase-H. Secretion of newly synthesized PAM-3 is detectable within 90 min after biosynthesis and is largely complete within 4 h. Release of the catalytic domains of PAM-1 and PAM-2, which requires endoproteolytic cleavage, occurs at a slow rate for many hours after biosynthesis. Release of PAM-3 and the soluble PAM proteins derived from PAM-1 and PAM-2 can be stimulated by secretagogue. Integral membrane PAM proteins that reach the surface of atrial myocytes are internalized and enter the endocytic pathway. The turnover of newly synthesized PAM-1 and PAM-2 is only partially accounted for by the release of soluble PAM protein into the medium and may involve a significant contribution from intracellular degradation.

Animals↗
PubMed1992

Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study.

Peptide alpha-amidation, an essential posttranslational modification that confers bioactivity to many neuroendocrine peptides, is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM; EC 1.14.17.3). To complement our previous studies on the distribution of PAM in neuroendocrine organs, we have examined expression of the PAM gene in several endocrine tissues by in situ hybridization and immunocytochemistry. In all instances, the autoradiographic densities for PAM mRNA correlated with staining patterns for PAM immunoreactivity. Very high levels of PAM mRNA were found in all heart atrial cardiomyocytes, while much lower levels were present in ventricular cells. In the sublingual gland, PAM was expressed diffusely in both acinar and tubule cells. In contrast, expression of PAM was confined to granular convoluted tubule cells in the submaxillary gland. PAM was expressed at high levels in a subset of adrenal medullary chromaffin cells, and low levels of PAM mRNA and immunoreactivity were also detected in the adrenal cortex. PAM was found predominantly in the calcitonin-producing parafollicular C-cells in the thyroid gland and in the glucagon-containing A-cells in the endocrine pancreas. Collecting and distal tubule cells of the kidney expressed both PAM mRNA and immunoreactivity. The basal cells in testicular seminiferous tubules containing PAM may represent developing germ and Sertoli cells. The cellular localization of PAM within the thyroid gland, adrenal gland, testis, and pancreas correlated with known peptidergic systems, and some of the observed cellular heterogeneity in PAM mRNA expression and immunoreactivity may reflect differences in the levels of amidated peptide production. The expression of PAM in cells not known to produce high levels of alpha-amidated peptides may indicate the production of yet unidentified alpha-amidated bioactive peptides or alternative functions of the PAM protein.

Adrenal Medulla↗
PubMed1989

Tissue specific expression of rat peptidylglycine alpha-amidating monooxygenase activity and mRNA.

The tissue specific expression of peptidylglycine alpha-amidating monooxygenase [(PAM) EC 1.14.17.3], an enzyme which catalyzes the formation of amidated bioactive peptides from their glycine-extended precursors, was examined in adult rat. Soluble and membrane-associated PAM enzymatic activities were determined, and the levels and size classes of PAM mRNA were examined by Northern blot analysis. PAM specific activity varied 1000-fold in the tissues examined, with highest levels in heart atrium, pituitary and salivary glands, and hypothalamus. The fraction of total PAM activity that was membrane associated varied from approximately 70% in heart atrium to 10% in neurointermediate pituitary lobe and thyroid gland. Levels of PAM mRNA varied over 300-fold. In the heart atrium, PAM mRNA accounts for more than 0.1% of the mRNA. For many tissues the ratio of total PAM specific activity to PAM mRNA levels was similar; however, PAM activity was higher than expected from mRNA levels in the salivary glands and lower than expected in several tissues, including heart ventricle. Three major size classes of PAM mRNA were identified among the tissues. Use of RNAse H indicated that differences in size were not due to the length of the poly(A) tail. The heart and central nervous system expressed PAM mRNA of the 4.2 kilobase (kb) and 3.8 kb size classes, while the remaining tissues expressed predominantly 3.8 kb and 3.6 kb classes; few tissues contained only one size class of PAM mRNA. The two major forms of PAM mRNA in adult heart atrium differ by the presence or absence of a 315 nucleotide segment in the protein coding region. Using a cDNA probe from within this segment, the 4.2 kb and 3.8 kb size classes of PAM mRNA in the central nervous system appeared to resemble those in the heart atrium. In the remaining tissues, a subset of PAM mRNAs in the 3.8 kb and 3.6 kb size classes hybridized with this probe, suggesting that additional forms of PAM mRNA are present.

Adrenal Glands↗
PubMed1994

Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase.

Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the COOH-terminal alpha-amidation of neuro-endocrine peptides through the sequential action of monooxygenase and lyase domains contained within this bifunctional protein. Alternative splicing leads to the expression of soluble and integral membrane bifunctional PAM proteins as well as a soluble monofunctional monooxygenase. In order to determine how alternative splicing affects post-translational modification of PAM proteins, we investigated the sulfation of PAM proteins expressed in stably transfected hEK-293 cells. Metabolic labeling with [35S]SO4(2-) or [35S]methionine and immunoprecipitation demonstrated that [35S]SO4(2-) was efficiently incorporated into PAM proteins that have the noncatalytic exon A region following the monooxygenase domain (PAM-1 and PAM-4) and into a soluble bifunctional PAM protein (PAM-3). Alkaline hydrolysis, radiosequencing, and deglycosylation experiments demonstrated the presence of a sulfated tyrosine (Tyr965) in the COOH-terminal domain of PAM-3 and multiple sulfated O-glycans in the exon A region of PAM-1 and PAM-4. A mutant PAM-3 protein in which Tyr965 was changed to Ala965 (PAM-3/Y965A) was not sulfated and exhibited monooxygenase and lyase activities similar to those of wild type PAM-3. Pulse-chase and temperature block experiments showed that the PAM-3/Y965A protein exits the trans-Golgi network faster than wild type PAM-3. Thus inclusion of exon A results in the sulfation of O-glycans, while elimination of the transmembrane domain results in the sulfation of Tyr965.

Alternative Splicing↗