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Biomedical subjects

J C Jørgensen

Publications and source records attributed to J C Jørgensen.

At least 19 recordsLinked to original sources

Verrucous endocarditis associated with Streptococcus bovis in mink (Mustela vison).

Between 1998 and 2001, mortalities due to verrucous endocarditis were experienced at several mink farms. Gram-positive cocci were isolated from the endocardium of all the animals examined but not always from other internal organs. Almost all the isolates were identified as Streptococcus bovis and only a few isolates belonged to other Streptococcus species. Typing by pulsed-field gel electrophoresis of a selection of isolates revealed several patterns and several different clones. Attempts to reproduce disease by the injection of cultures of a field isolate into healthy mink failed.

Animals↗

Pasteurella multocida from outbreaks of avian cholera in wild and captive birds in Denmark.

An outbreak of avian cholera was observed among wild birds in a few localities in Denmark in 2001. The highest mortalities were among breeding eiders (Somateria mollissima) and gulls (Larus spp.). Pulsed-field gel electrophoresis (PFGE) was conducted using ApaI and SmaI as restriction enzymes and restriction enzyme analysis (REA) using HpaII. The Pasteurella multocida subsp. multocida strain isolated from birds in this outbreak was indistinguishable from a strain that caused outbreaks in 1996 and 2003. Most isolates from domestic poultry had other PFGE patterns but some were indistinguishable from the outbreak strain. Among 68 isolates from wild birds, only one PFGE and one REA pattern were demonstrated, whereas among 23 isolates from domestic poultry, 14 different SmaI, 12 different ApaI, and 10 different HpaII patterns were found. The results suggest that a P. multocida strain has survived during several years among wild birds in Denmark.

Animals↗

Serovars of Salmonella isolated from Danish turkeys between 1995 and 2000 and their antimicrobial resistance.

The prevalence of Salmonella serovars and their antimicrobial resistance patterns were investigated among Danish turkeys between 1995 and 2000, by sampling the flocks approximately 14 days before they were slaughtered. Within the flocks, the prevalence of salmonella varied from 7.1 per cent to 25 per cent, and 24 different serovars were detected. The five most prevalent, which accounted for 58.5 per cent of the isolates were Salmonella Heidelberg (16.2 per cent of the isolates), Salmonella Agona (15.8 per cent), Salmonella Derby (12.4 per cent), Salmonella Muenster (7.3 per cent) and Salmonella Anatum (6.8 per cent). In addition, a few rough isolates and isolates belonging to the antigenically incomplete formulae 6,7:-:- and 4,12:b:- were found. The level of antimicrobial resistance was low; the highest resistance was recorded to ampicillin (13.7 per cent) and streptomycin (9.0 per cent) followed by tetracycline (8.5 per cent), sulphonamides (7.7 per cent) and spectinomycin (4.7 per cent). Resistance to quinolones was very low: four isolates were resistant to nalidixic acid, and only one was resistant to enrofloxacin. No resistance was recorded to colistin, apramycin, ceftiofur, florfenicol, or amoxycillin with clavulanic acid. Only 24 isolates were resistant to two or more compounds in various combinations of up to six compounds; one Salmonella Havana isolate was resistant to six compounds. Six isolates were serovar Typhimurium, but none of them belonged to phage type DT104.

Animals↗

Pre-harvest surveillance of Campylobacter and Salmonella in Danish broiler flocks: a 2-year study.

In national surveillance programmes of broiler flocks carried out in Denmark during 1998 and 1999, 89,110 samples for Campylobacter representing 8911 broiler flocks were taken at 10 different abattoirs, and 44,550 samples for Salmonella were taken from the same flocks in the broiler houses at the farms. Of the swabs, 42.5% were Campylobacter positive. Most positive samples were found during July, August and September, while the lowest number of positive samples were found during January, February, March and April. Of the flocks, 5.5% were Salmonella positive, but no seasonal variation was observed. For each flock, the presence of Campylobacter and Salmonella was recorded in order to estimate the possible correlation between colonisation with the two pathogens. In conclusion, no significant effects on intensive cleaning and disinfection procedures on Campylobacter occurrence could be demonstrated, and no significant correlation between occurrence of Campylobacter and Salmonella infections in Danish broilers could be demonstrated which is in contrast to previous observations on concurrent colonisation of broilers with these two zoonotic pathogens.

Abattoirs↗

The effect of neuropeptides on vessel tone and cAMP production.

The effect of VIP, PHM, PHV, PACAP-27, and PACAP-38 on vessel tone and cAMP production was investigated in rabbit ovarian arteries in vitro. The peptides (10(-7)M) induced a significant relaxation on NA-precontracted vessels and displayed similar potencies. The cAMP accumulation induced by PACAP-27 and PACAP-38 was five times higher than the cAMP content induced by VIP, PHM, and PHV. NPY (10(-7)M) markedly reversed the relaxations induced by VIP, PHM, PHV, PACAP-27, and PACAP-38 but did not at all affect the cAMP production induced by these peptides. We conclude that the relaxation induced by VIP, PHM, PHV, PACAP-27, and PACAP-38 and the contraction evoked by NPY are not solely related to the changes of cAMP contents, and that in addition to cAMP, another intracellular signal transduction pathway may be involved.

Animals↗

Pituitary adenylate cyclase activating polypeptide (PACAP): occurrence and vasodilatory effect in the human uteroplacental unit.

UNLABELLED: Pituitary adenylate cyclase activating polypeptide (PACAP) is a neuropeptide which was originally isolated from ovine hypothalamus. PACAP exists in at least two biologically active forms, PACAP-38 and PACAP-27. The aim of this study was to establish the distribution, localization and smooth muscle effects of PACAP-38 and PACAP-27 in the human uteroplacental unit. For this purpose we used radioimmunoassay, immunocytochemistry and in vitro studies of the effect of the peptides on smooth muscle activity. RESULTS: By radioimmunoassay both peptides were detected throughout the uteroplacental unit. The concentrations of PACAP-27 were in general low, ranging from 1/6-1/25 of the corresponding PACAP-38 concentrations. PACAP-immunoreactivity was localized in nerve fibres of the lower segment of the pregnant uterus, but the number of PACAP-immunoreactive nerves was very clearly reduced compared to the corresponding isthmic region of non-pregnant myometrial tissue. PACAP-immunoreactive fibres were not observed in placenta or in the umbilical cord. Both PACAP-38 and PACAP-27 caused a concentration-dependent relaxation on stem villous arteries and on the intramyometrial arteries. Neither of the peptides displayed any effect on non-vascular smooth muscle specimens from the term pregnant myometrium. In conclusion the findings suggest a vasoregulator role of PACAP in the human uteroplacental unit.

Adult↗

Vascular effects and cyclic AMP production produced by VIP, PHM, PHV, PACAP-27, PACAP-38, and NPY on rabbit ovarian artery.

The relationship between vessel tone and cAMP production induced by vasoactive intestinal polypeptide (VIP), peptide histidine methionine (PHM), peptide histidine valine (PHV), pituitary adenylate cyclase activating polypeptide (PACAP-27 and PACAP-38), and neuropeptide Y (NPY) was investigated in rabbit ovarian arteries in vitro. VIP, PHM, PHV, PACAP-27, and PACAP-38 added in single-dose experiments (10(-9), 10(-8), 10(-7), and 10(-6) M) induced all a significant dose-related relaxation of noradrenaline (NA)-precontracted vessels and displayed similar potencies. VIP, PHM, PHV, PACAP-27, and PACAP-38 all increased cyclic adenosine monophosphate (cAMP) accumulation. The cAMP accumulation induced by PACAP-27 and PACAP-38 was five times higher than the cAMP content induced by the other three peptides. The peptide-induced smooth muscle relaxation did not correlate to the cAMP accumulation. NPY (10(-7) M) markedly reversed the relaxations induced by VIP, PHM, PHV, PACAP-27, and PACAP-38, but did not influence the cAMP production induced by these peptides. In conclusion, the relaxation induced by VIP, PHM, PHV, PACAP-27, and PACAP-38 and the contraction induced by NPY are not solely related to the changes of cAMP contents. These findings indicate that in addition to cAMP, another intracellular signal transduction pathway may be involved in the relaxation and contraction induced by these peptides in rabbit ovarian artery.

Animals↗

Neuropeptide Y in the human prenatal and mature gonads.

In the present paper we have examined the distribution and identity of neuropeptide Y (NPY) immunoreactivity in the prenatal and mature human gonads. Tissue specimens were obtained from prenatal gonads (gestational age < 42 weeks) of induced abortions, premature birth and stillbirths. Specimens were also taken from infants who died aged less than 4 days. Tissue from mature gonads was obtained during surgery. The distribution and concentration in tissue extracts were determined by immunohistochemistry and radioimmunoassay. NPY-immunoreactivity (NPY-IR) was demonstrated in both the prenatal and mature human gonads. In the gonads from fetuses at 16-25 weeks the NPY-IR was scarce and could only be demonstrated by radioimmunoassay. In the female gonads from fetuses at 40 weeks of gestation, distinct nerve fibres were detected in relation to blood vessels and primordial follicles. In the prenatal male gonads at the same gestational length as well as in the mature testis, the NPY-IR nerves were detected in relation to blood vessels and seminiferous tubules. The gel filtration profile from the prenatal gonads and from the mature ovary revealed a single peak corresponding to the elution position of bioactive synthetic human NPY. The gel filtration profile from the mature testis demonstrated an additional peak at Kd of 0.17. The presence of NPY-IR in relation to the developing and mature gonads suggests that NPY participates in gonadal functions from an early point in life.

Chromatography, Gel↗

Stimulation of rainbow trout gallbladder contraction by cionin, an ancestral member of the CCK/gastrin family.

Cionin--from the protochordate Ciona intestinalis--is a putative ancestor of cholecystokinin (CCK) and gastrin. Being sulfated on tyrosine in positions 7 and 6 (from the C-terminus), characteristic for CCK and gastrin, respectively, cionin is a structural hybrid of the two peptides. The effects of cionin have previously been characterized in mammalian systems. This study examined a phylogenetically ancient CCK receptor, the rainbow trout (Oncorhynchus mykiss) gallbladder receptor, utilizing cionin, sulfated and nonsulfated CCK and gastrin, and the receptor antagonists L-364,718 and L-365,260. The sulfated peptides induced concentration-dependent contractions of isolated strips of gallbladder with equal efficacy and similar potencies [ED50: 42 (cionin), 23 (CCK-8-s), and 74 nM (gastrin-17-s)], significantly different from the nonsulfated forms [ED50: 1.7 (CCK-8-ns) and 1.9 microM (gastrin-17-ns)]. Ten micromolar L-364,718 and L-365,260 both weakly but significantly inhibited cionin-CCK-8-s, and gastrin-17-s-induced contractions. L-365,260 shifted the concentration response curves 1 1/2 decades to the right and L-364,718 only 1/2 decade. The results confirm that the rainbow trout gallbladder CCK receptor does not distinguish sulfated CCK from sulfated gastrin as do modern CCKA receptors, but does distinguish sulfated from nonsulfated forms of both. However, for optimal effect the receptor does not require a double-sulfated peptide like cionin as might be expected from the lack of selectively between CCK and gastrin. Finally, studies with antagonists known to be specific for either CCK or gastrin receptors in mammalian systems indicate that this ancient receptor behaves more like a mammalian CCKB receptor than as a CCKA receptor.

Amino Acid Sequence↗

Pituitary adenylate cyclase-activating polypeptide: occurrence and relaxant effect in female genital tract.

The distribution, localization, and smooth muscle effects of pituitary adenylate cyclase-activating polypeptide (PACAP) were studied in the human female genital tract. The concentrations of PACAP-38 and PACAP-27 were measured by radioimmunoassays, and both peptides were found throughout the genital tract. The highest concentrations of PACAP-38 were detected in the ovary, the upper part of vagina, and the perineum. The concentrations of PACAP-27 were generally low, in some regions below the detection limit and in other regions 1 to 5% of the PACAP-38 concentrations. Immunocytochemistry revealed that PACAP was located in delicate varicose nerve fibers that were most abundant in the internal cervical os, where they mainly seemed to innervate blood vessels and smooth muscle cells. PACAP-38 and PACAP-27 (10(-10)-10(-6) M) caused a concentration-dependent relaxation of the spontaneous activity of the nonvascular smooth muscle strips from fallopian tube and myometrium in vitro. Likewise, both peptides (10(-10)-10(-6) M) caused relaxation of nonrepinephrine (10(-6) M)-precontracted intramyometrial arteries. No effect of the PACAP sequences, PACAP-(6-27), PACAP-(16-38), and PACAP-(18-27), on fallopian tube was observed. The findings suggest a smooth muscle regulatory role of PACAP in the human female reproductive tract.

Adolescent↗

Pituitary adenylate cyclase activating polypeptide induces vascular relaxation and inhibits non-vascular smooth muscle activity in the rabbit female genital tract.

In vitro effects of two bioactive forms of pituitary adenylate cyclase activating polypeptide (PACAP): PACAP-38 and PACAP-27 were studied on rabbit vascular and non-vascular smooth muscle. Segments of the ovarian artery and muscle strips from the fallopian tube were used. Two series of experiments were performed on vessels: the dose-response relationship of PACAP-38 (10(-10)-10(-7) M) was established on noradrenaline- (NA, 10(-6) M) contracted vessels. In the other set of experiments the contractile effect of 10(-8)-10(-4) M NA added cumulatively, was studied on arterial segments incubated with PACAP-38 (10(-7) M), PACAP-27 (10(-7) M) or VIP (10(-7) M). The effect of PACAP-38, PACAP-27 and VIP (10(-10)-10(-6) M) was investigated on spontaneously contracting smooth muscle of the fallopian tube. Longitudinally as well as transversally cut specimens were investigated. PACAP-38 produced a significant dose-related relaxation on the NA-precontracted vessels. However, pre-incubation of the vessels with 10(-7) M PACAP-38, PACAP-27 and vaso active intestinal polypeptide (VIP) did not induce a general rightward shift of the NA concentration-response curves, although a tendency to inhibition in the low-dose interval was observed. The peptides caused a significant, dose-dependent inhibition of both frequency and amplitude on the fallopian tube smooth muscle activity. The effects of the three peptides on longitudinally as well as transversally cut specimens were alike.

Animals↗

Neuropeptide Y in mammalian genital tract: localization and biological action.

Neuropeptide Y, NPY, is one of the most common neuropeptides in mammalian and seems to influence many physiological systems significantly, e.g. the cardiovascular system and the gastrointestinal system. In the present investigation the distribution, localization and physiological effects of NPY were studied in the mammalian genital tract, primarily the female. In the human female genital tract the highest concentrations of NPY-immunoreactivity, NPY-IR, measured by radioimmunoassay, were demonstrated in the uterine artery, the ovary, the Fallopian tube, and the vagina. Immunohistochemical investigations demonstrated the highest density of NPY immunoreactive nerve fibers in relation to blood vessels, although some NPY-IR nerves also were seen close to non-vascular smooth muscle. In the ovary, many NPY-IR nerves were observed in connection with follicles. The NPY-IR material throughout the genital tract was identical to synthetic, amidated human NPY as evaluated by gel filtration, high performance liquid chromatography, and isoelectric focusing. Pro-NPY and NPY-IR material was also demonstrated in human plasma and follicular fluid. NPY induced only a weak direct contractile effect on small cervical arteries from humans investigated in vitro by isometric tension measurements. NPY had no effect on smooth muscle specimens either from the salpinx or the uterus. The 133Xe washout method was evaluated on the rabbit ovary in order to measure changes in the ovary blood flow rate in vivo. A mono-exponential washout curve for 133Xe was found for the whole washout process, ensuring that the blood flow rate at any time could be calculated from the curve. Injection of NPY close to ovarian artery resulted in a dose dependent decrease in the ovarian blood flow rate with a maximum reduction to 40% of the control blood flow rate. In vitro investigation of the rabbit ovarian artery demonstrated only a weak direct contractile effect of NPY but a significant potentiation of the NA response was observed. In vessels precontracted with NA, it was demonstrated that NPY was a potent inhibitor of vasoactive intestinal peptide-induced relaxation. The postsynaptic contractile NPY effects in the rabbit ovarian artery were most likely mediated through a NPY Y1 receptor as demonstrated by the effect of the selective NPY Y1 receptor agonist [Leu31,Pro34]NPY and the Y2 receptor agonist, NPY11-36. The presynaptic inhibitory effect of NPY on the vas deferens motor response induced by electrical stimulation was possibly caused by stimulation of NPY Y2 receptors as evaluated by the effect of the above mentioned peptide analogs in this system.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

Neuropeptide Y (NPY) in human penile corpus cavernosum tissue and circumflex veins--occurrence and in vitro effects.

The concentration and distribution of neuropeptide Y (NPY) within the penile corpus cavernosum (CC) and in penile circumflex veins (CV) from healthy potent males was investigated by immunochemistry and immunohistochemistry. The concentrations were assessed to 28.6 pmol/gm. (CC) and 15.8 pmol/gm. (CV) respectively. Gel filtration on CC tissue extracts demonstrated a single peak of NPY-immunoreactivity (NPY-IR) similar to synthetic human NPY. The NPY-IR was confined to nerve fibers seemingly innervating smooth muscle cells. In vitro myographic examinations demonstrated contractile activation by NPY in 2/8 CC strips and in 5/8 CV strips. The mean contractile force was 1.17 +/- 0.62 mN (18.3 +/- 15.8% of the K(+)-induced contraction) and 2.42 +/- 0.42 mN (31 +/- 12%) respectively. NPY 10(-7) and 10(-6) M displayed a potentiating effect on the response to NA 10(-9) in one of six CC and four of six CV preparations. It is suggested that NPY could add to the contractile effect of NA in detumescence and in maintenance of the resting state; contribution of NPY to the veno-occlusive mechanism at initiation of erection is another putative physiological function.

Adult↗

Effect of regulatory peptides on the blood flow rate in rabbit female genital tract evaluated by the 133Xe technique.

The 133Xe washout method has been evaluated and found to be a reliable method for the measurement of myometrial as well as ovarian blood flow rates in the rabbit. Monoexponential washout curves for 133Xe have been demonstrated for the whole washout process, both in the uterus and the ovary. Consequently it is possible to calculate the blood flow rate at any time interval during the whole washout process. This 133Xe washout technique has been used for the evaluation of the biological effect of neuropeptides on the local blood flow within the rabbit uterus and ovary. It has been recognized for years that the intrinsic control of a number of functions, including the blood flow regulation, in the genital tract cannot be attributed to cholinergic and/or adrenergic nerves alone. Evidence from 133Xe experiments suggests that the neuropeptides in the female genital tract may play a functional role in these non cholinergic non adrenergic events.

Animals↗

Structure-function studies on neuropeptide Y and pancreatic polypeptide--evidence for two PP-fold receptors in vas deferens.

The biological effects of neuropeptide Y (NPY), rat pancreatic polypeptide (rPP), hybrid analogs of NPY and PP, and C-terminal fragments of NPY were studied in the field-stimulated rat vas deferens model. The results were correlated with peptide binding experiments in Y1 and PP receptor assays on rat PC-12 cells and Y2 receptors on porcine hippocampal membranes. NPY and rPP inhibited the electrically induced contractions in the vas deferens with an IC50 of 25 and 22 nM respectively. However, in contrast to NPY, rPP could not totally block muscle activity. The inhibitory action of the long C-terminal fragment of NPY, NPY-(19-36) and NPY-(11-36), indicated that NPY acts through a Y2 receptor in the vas deferens. The structural basis for the differential recognition of NPY and PP by Y2 receptors and partly also by PP receptors, could be defined with hybrid analogs of PP and NPY. The analogs, [Ile31,Gln34]PP and [Leu31,Pro33]NPY reacted in the vas deferens preparation in accordance with their relative potency in the Y2 and PP receptor assays. [Ile31,Gln34]PP, which bound to the Y2 receptor like NPY, was also able to block the part of the contractile response which was resistant to rPP. It is concluded that in the vas deferens, PP-fold peptides act through two types of receptors: Y2 and PP, and that residues in the C-terminal part of the molecules determine the differential recognition of the peptides by these receptor types.

Amino Acid Sequence↗

Demonstration of neuropeptide Y and its precursor in plasma and follicular fluid.

The present investigation provides three lines of evidence for the presence of a pro-form of neuropeptide Y (NPY) in plasma and follicular fluid. First, by the demonstration of NPY-immunoreactive material of a size corresponding to the estimated mol wt of pro-NPY. Second, an antiserum specific for the C-terminal tyrosine amide of NPY and peptide YY does not react with this material. Third, it was possible to convert the pro-NPY extracted from plasma and follicular fluid using the protease, Endoproteinase-Lys C, to a NPY-immunoreactive form eluting slightly before NPY on a G-50 column. The size of the digested product was consistent with a cleavage of pro-NPY resulting in an immunoreactive species, NPY-Gly-Lys. Pro-NPY was also found in tissue culture media from the human neuroendocrine cell line SH-SY5Y. As in the case of plasma and follicular fluid, another NPY immunoreactive species eluted from a G-50 gel filtration column slightly before synthetic human NPY. Analysis of this material with an antibody directed against the tyrosine amide of NPY in combination with isoelectric focusing revealed that this peak consisted of at least two immunoreactive forms of NPY. In conclusion, at least three different forms of NPY immunoreactivity are likely to be present in plasma, follicular fluid, and cell tissue culture media; pro-NPY, a degradation form of pro-NPY, or a biosynthetic intermediate and NPY.

Chromatography, Gel↗

Seasonal variation of serum bone GLA protein.

The seasonal variation of serum Bone Gla Protein (BGP) was investigated in 15 normal young individuals (seven women and eight men, aged 27-39 years). Serum BGP exhibited a significant seasonal variation of 23% around the yearly mean (p less than 0.001) with zenith in February and nadir in July. Significant seasonal variations were noted also for serum alkaline phosphatase (p less than 0.01) and serum phosphate (p less than 0.01). Serum calcium, bone mineral content (BMC) and creatinine clearance revealed no significant seasonal variation. The seasonal variation of BGP did not follow the variation in serum total alkaline phosphatase. The seasonal variation of BGP has to be taken into account when using the protein as a marker of bone remodelling activity. The variation was probably caused by changes in the production rate of the protein, since the renal excretion of the protein, as reflected in creatinine clearance, remained unchanged throughout the year.

Adult↗

Neuropeptide Y in the human female genital tract: localization and biological action.

The distribution, localization, and smooth muscle effects of neuropeptide Y (NPY) were studied in the human female genital tract. High concentrations of NPY immunoreactivity were demonstrated in the uterine artery, the ovary, the fallopian tube, cervix, and the vagina. The NPY immunoreactivity was confined to nerve fibers. The highest density of nerve fibers was observed in relation to blood vessels, although some NPY-immunoreactive nerves were also seen close to nonvascular smooth muscle. The NPY-immunoreactive material throughout the genital tract was identical to synthetic amidated human NPY with regard to size, hydrophobicity, and charge as evaluated by gel filtration, high-performance liquid chromatography, and isoelectric focusing. NPY (10(-10) to 10(-6) M) exerted a direct vasoconstrictory effect on small arteries dissected from the cervix and an additive effect of NPY and norepinephrine responses was observed. Exogenous NPY did not have a direct effect on nonvascular smooth muscle specimens from the fallopian tube or the myometrium. The close relation between NPY-immunoreactive nerves and blood vessels, the presence of NPY-immunoreactive material identical to amidated synthetic human NPY, and the vasoconstrictory effects of NPY indicate that NPY is involved in the regulation of the blood flow in the human female genital tract.

Antibodies↗