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Biomedical subjects

K Dahlbäck

Publications and source records attributed to K Dahlbäck.

18 recordsLinked to original sources
PubMed2005

Familial brachioradial pruritus.

BACKGROUND: The cause of brachioradial pruritus (a localized itching on the arms or shoulders) is controversial. A hereditary form of this condition has not been reported. OBJECTIVES: To describe the occurrence of brachioradial pruritus in several members of one family. PATIENTS AND METHODS: The pedigree of the three generations and the history of brachioradial pruritus was outlined. Four sisters were investigated by radiography of the cervical spine. RESULTS: Five sisters and one brother, together with five of their daughters suffered from recurring brachioradial pruritus. The sisters had had occupations requiring heavy lifting, spent much time outdoors and exposed themselves extensively to the sun. Several complained of neck pain and cervical radiographs of four of them indicated arthrosis. CONCLUSIONS: Spinal disease alone cannot explain the symptoms of brachioradial pruritus, which in our patients was characterized by symptom-free periods broken off by relapse late in the summer each year. The pedigree suggests this hereditary form of brachioradial pruritus to be dominant and possibly X-linked.

Adolescent↗
PubMed1995

Clinical and immunohistochemical findings in a case of neonatal Marfan syndrome.

A newborn girl with extreme cardiomegaly discovered by fetal ultrasound after 34 gestational weeks is presented. The girl was delivered through a Caesarean section. After birth, multiple skeletal stigmata and generalized cardiac involvement with abnormal valves and dilated great arteries suggested Marfan syndrome. The girl died at the age of 10 h. The postmortem examinations showed cardiovascular lesions typical of Marfan syndrome. Immunofluorescence studies from cultured fibroblasts of the patient showed decreased amounts of immunostained fibrous material, supporting the clinical diagnosis of a severe Marfan syndrome.

Antibodies, Monoclonal↗
PubMed1993

Vitronectin in mouse skin: immunohistochemical demonstration of its association with cutaneous amyloid.

Vitronectin is a multifunctional glycoprotein known to be associated with the dermal elastic fiber network in human adults, with various types of human amyloid and with apoptotic keratin bodies in human skin. It has also been shown to bind to human keratin intermediate filaments and to intranuclear material in vitro. To learn more of its function and mode of tissue deposition, vitronectin in mouse skin was studied. Vitronectin was purified from mouse plasma and a polyclonal anti-vitronectin antiserum was produced. This was used in an avidin-biotin-peroxidase complex technique and in an immunofluorescence technique on biopsy sections of dorsal skin from mice. Hairless lightly pigmented mice, known to develop dermal amyloid deposits at advanced ages, were used, making it possible to study vitronectin's association not only with elastic fibers but also with amyloid. Association of vitronectin with elastotic material was investigated in mice exposed to ultraviolet radiation. No vitronectin immunoreactivity could be demonstrated in association with elastin-stained material in skin specimens from any of the mice, whether exposed to ultraviolet radiation or not. In contrast, vitronectin was constantly found to be associated with dermal amyloid deposits. Moreover, mouse vitronectin was found to bind to mouse keratinocytes when studied by immunofluorescence staining of skin sections that had been pre-incubated with mouse plasma as sources of vitronectin. The results indicate that vitronectin is associated with amyloid and can bind to intracellular structures in epidermal keratinocytes in mice as in humans, and that mouse tissue may be used for the study of vitronectin's interactions with amyloid and with intracellular structures.

Amino Acid Sequence↗
PubMed1991

Tissue vitronectin in normal adult human dermis is non-covalently bound to elastic tissue.

Vitronectin is a multifunctional human plasma glycoprotein that is also found in constant association with elastic tissue fibers in normal adults. We have investigated the nature of the association of vitronectin with elastic tissue, and compared it to that of other elastic fiber-associated proteins, namely fibrillin and amyloid P component. Samples of normal human dermis were incubated with a variety of extraction agents, including high molar salt solution, non-ionic detergent (Nonidet P-40), the reducing agents dithiothreitol or 2-mercaptoethanol, and the chaotropic agents sodium dodecyl sulfate or guanidine hydrochloride. Vitronectin purified from serum typically migrates as two bands of 75 and 65 kD. By contrast, immunoblotting studies of residual dermal material after extraction with the various agents revealed only lower molecular weight (58, 50, 42, 35, and 27 kD) anti-vitronectin reactive bands. Although these bands may represent degradation products of vitronectin generated as a result of the extraction procedure, we cannot exclude the possibility that tissue vitronectin is distinct from plasma vitronectin. Anti-vitronectin reactive polypeptides co-migrating with the 58-, 50-, and 42-kD bands were solubilized following extraction with sodium dodecyl sulfate or guanidine hydrochloride, but not with the other extraction agents. Immunofluorescence studies using residual dermal material after extraction with guanidine hydrochloride demonstrated a marked reduction in elastic fiber staining intensity with anti-vitronectin and anti-amyloid P component, but not with anti-fibrillin. Thus the majority, if not all of dermal vitronectin, is, like amyloid P component, non-covalently associated with, and not an integral constituent of, elastic fibers.

Blood Proteins↗
PubMed1991

Elastolysis in lichen ruber planus.

The dermal elastic fiber network was studied in specimens from five patients with lichen ruber planus, using a standard elastin staining procedure (orcein), results being compared with those for the elastin-associated microfibrillar network stained using anti-fibrillin antibodies in an immunofluorescence and an avidin-biotin-peroxidase complex technique. Additional specimens of healed apparently normal skin were taken from two of the patients. Orcein-stained fibers were scarce or absent in the inflammatory zone in all the lesions. In contrast, an extensive fibrillin immunoreactive network was present in the papillary zone in all the specimens, in a pattern similar to that of normal skin. In specimens from healed lesions of lichen ruber planus, dermal orcein-stained fibers were present in the papillary dermis. The findings indicate that the amorphous component of elastic fibers is destroyed during the acute phase of lichen ruber planus. Hypothetically, the elastolysis is caused by elastases released from macrophages known to be present in the lichenoid infiltrate. In contrast, the fibrillin fiber network seems to be less or not at all affected by proteolytic events during the inflammatory phase of lichen ruber planus.

Acute Disease↗
PubMed1991

[Vitronectin in normal human skin and in skin lesions].

Vitronectin (S-protein of complement, serum spreading factor) is a multifunctional glycoprotein present in human plasma and in the elastic tissue of various organs. It belongs to the group of adhesion proteins and is of importance in the terminal stages of both the coagulation and complement system and in fibrinolysis. In human skin it is localized on dermal elastic fibers and on pathologically altered elastic material (solar elastosis, pseudoxanthoma elasticum) as well as on keratin filament material such as keratin bodies in lichen planus or amyloid deposits in localized cutaneous amyloid. It is also found in the abnormally thickened cutaneous blood vessels in erythropoietic protoporphyria and porphyria cutanea tarda. Late-stage inhibition of the complement cascade in bullous disorders in which activation of the complement system is of pathogenetic significance may be an additional important function of vitronectin in skin diseases.

Blood Coagulation↗
PubMed1991

Middermal elastolysis. Report of a case and immunohistochemical studies on the dermal distribution of fibrillin, vitronectin and amyloid P component.

A 39-year-old woman with demarcated wrinkled areas, histologically characterized by absence of elastic fibers in the middle and upper reticular dermis, is described. Immunoreactivity of vitronectin and amyloid P component, present at the periphery of elastic fibers in normal skin in adults, was absent from the middermis of lesional skin as were orcein stained fibers. C9 neoantigen immunoreactivity, associated with elastic fibers in sun-exposed skin of middle-aged and elderly individuals, was present in conjunction with elastic fibers in papillary and lower reticular dermis in lesional skin but was absent in the middermis. In contrast, a fibrillin immunoreactive network was present throughout the dermis, indicating that the elastin-associated microfibrils are retained in the absence of amorphous elastin in lesional skin of middermal elastolysis.

Adult↗
PubMed1990

Fibrillin immunoreactive fibers constitute a unique network in the human dermis: immunohistochemical comparison of the distributions of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis.

Fibrillin, a 350-kD glycoprotein, was recently localized to elastin-associated 10 nm microfibrils. Here, the distribution of fibrillin immunoreactivity was determined in normal skin in individuals of different ages and in lesions of solar elastosis or anetoderma. It was compared with the distribution of orcein-stainable fibers and with the immunoreactivities of vitronectin and amyloid P component. These glycoproteins are known to occur in conjunction with the orcein-stainable elastic fibers in adults, but not in the young. Fibrillin immunoreactivity was associated with orcein-stainable fibers in normal skin of both adults and the young. In addition, the fibrillin immunoreactive fiber network comprised fine fibers that were unstainable by orcein, anti-vitronectin, or anti-amyloid P component. Such fine fibers were especially abundant close to the dermal-epidermal junction zone. Immunoreactivities of anti-vitronectin and anti-amyloid P component were not always associated with fibrillin immunoreactivity but were consistently found to co-localize with orcein-stainable fibers in adults. This suggests vitronectin and amyloid P component to be associated with the amorphous elastin rather than with the microfibrils, although alternative interpretations are possible. In elastotic lesions, fibrillin immunoreactivity was generally fainter than that obtained using anti-vitronectin or anti-amyloid P component. In contrast, an extensive network of dermal fibers stained by anti-fibrillin, but not by anti-amyloid P component, anti-vitronectin, or orcein, was seen in an anetoderma lesion. In conclusion, fibrillin immunoreactivity is associated with a unique dermal network, which ultrastructurally is composed of microfibrils. These fibers are proposed to have an important structural and functional role in anchoring the dermal elastic fibers in the extracellular matrix and to the lamina densa.

Connective Tissue Diseases↗
PubMed1990

Deposition of C3, C9 neoantigen and vitronectin (S-protein of complement) in lichen planus pemphigoides.

We have compared the distribution of C3, C9 neoantigen (C9n) and vitronectin at the dermoepidermal junction in lichen planus pemphigoides with that in bullous pemphigoid. Eight out of 30 biopsies from patients with lichenoid lesions had linear C3 deposition at the basement membrane zone (BMZ); four of these patients had bullae and fulfilled the criteria for lichen planus pemphigoides. C9n immunoreactivity was detected as a linear or an intermittent linear/granular band at the BMZ only in these four patients, suggesting a role for the membrane attack complex of complement (MAC) in the pathogenesis of blister formation in lichen planus pemphigoides. Faint linear deposition of vitronectin, in addition to C9n, at the BMZ was seen in two of the four cases of lichen planus pemphigoides and three of six cases of bullous pemphigoid. This suggests that vitronectin may be deposited in association with C9n not only as part of the non-lytic SC5b-9 complex, but also as a regulatory step following the lytic action of MAC. A regulatory function for vitronectin in limiting tissue damage following activation of MAC is supported by our finding of a heavy deposition of vitronectin in association with C9n in a lichen planus pemphigoides patient in whom bulla formation had ceased.

Adult↗
PubMed1990

IgA immunoreactive deposits collocal with fibrillin immunoreactive fibers in dermatitis herpetiformis skin.

The IgA immunoreactive granules or fibrils, characteristically found in dermal papillae of patients with dermatitis herpetiformis, were previously reported to be associated with microfibrillar bundles. Recently, fibrillin, a component of such 8-12 nm microfibrils, was identified. In normal skin, the fibrillin immunoreactive microfibrils are present at the periphery of elastic fibers and are also present without concomitant amorphous elastin in the dermal papillae close to the lamina densa. The localization of the IgA immunoreactive material in the dermal papillae of 17 patients with dermatitis herpetiformis was compared with the distribution of the fibrillin immunoreactive fiber network. Immunofluorescence methods using FITC- and TRITC-labelled antibodies, an avidin-biotin-peroxidase complex technique, and standard elastin staining procedures, were used in several sequential and double staining procedures. In 13 specimens, in which the IgA reactivity was granular, most of the granules were located at the sites of fibrillin-reactive structures. As it could not be excluded that the collocality was coincidental, it could not be ascertained whether the IgA granules were in fact related to the fibrillin immunoreactive fibers in these specimens. However, in 4 specimens with both granular and fibrillar IgA immunoreactive deposits, these were clearly related to and located at the sites of fibrillin-reactive fibrils in the dermal papillae. The results confirm earlier reports of an association of IgA reactive deposits with microfibrillar bundles in dermatitis herpetiformis skin, though the possibility of their binding to other extracellular matrix component(s) has not been ruled out. The findings suggest that fibrillin may be the structural component (or one of them) to which IgA reactive deposits bind in the skin of patients with dermatitis herpetiformis.

Complement C3↗
PubMed1990

Immunohistochemical studies on fibrillin in amyloidosis, lichen ruber planus and porphyria.

The pathogenesis of macular amyloidosis and lichen amyloidosis remains unsolved and the primary amyloid fibril protein(s) has not yet been identified. Ultrastructural association of skin amyloid with elastin associated microfibrils has been noted earlier. The presence of fibrillin in conjunction with such microfibrils was recently demonstrated immunohistochemically. The presence of fibrillin immunoreactivity in the amyloid deposits in skin biopsies from 3 patients with macular amyloidosis and 3 patients with lichen amyloidosis was studied, using monoclonal anti-fibrillin antibodies. For comparison, skin specimens were studied from five patients with lichen ruber planus, four patients with erythropoietic protoporphyria and from a patient with myeloma-associated cutaneous amyloidosis. Renal specimens from two cases of the amyloid A type of renal amyloidosis also were investigated. There was no immunostaining either of the keratin bodies in specimens of lichen ruber planus, the cutaneous PAS-positive vascular deposits in patients with erythropoietic protoporphyria, or the amyloid deposits in specimens of systemic amyloidosis and it was faint or absent in amyloid deposits in the specimens from patients with lichen amyloidosis. In contrast, distinct fibrillin immunoreactivity could be demonstrated in amyloid deposits in specimens from patients with macular amyloidosis. It was sometimes absent in deposits located in the upper part of the papillary dermis, close to the dermal epidermal junction zone, while consistently strong in deposits located lower down in the dermis. The results suggest that fibrillin or part of the fibrillin molecule may be present in some of the amyloid deposits in specimens of macular amyloidosis.

Amyloidosis↗
PubMed1989

Vitronectin shows complement-independent binding to isolated keratin filament aggregates.

Keratinocyte cell death, whether produced by skin disease or by physiologic apoptosis in normal skin, may result in formation of dermal keratin bodies, consisting mainly of keratin intermediate filament aggregates. Vitronectin, a multifunctional plasma and tissue glycoprotein, which inhibits the complement membrane attack complex and promotes cell attachment and spreading, is, like amyloid P component, associated with keratin bodies in vivo. To investigate a potential role for vitronectin in the removal of keratin bodies, we studied the interaction of vitronectin with keratin intermediate filaments in normal human skin and in Hep-2 cells, as well as with isolated keratin intermediate filament aggregates in vitro. Following pre-incubation of skin sections and Hep-2 cells with normal human serum (as a source of vitronectin), cytoplasmic staining of keratinocytes and of cytoskeletal filaments in Hep-2 cells was observed by immuno-fluorescence staining with polyclonal and monoclonal anti-vitronectin antibodies. Vitronectin binding to keratin intermediate filament aggregates extracted from normal human epidermis was demonstrated by immunofluorescence and by immunoblotting, and was not dependent on complement activation, because it occurred even when heat-inactivated human serum or C4-deficient serum was used as a source of vitronectin. Amyloid P component shows Ca++- dependent binding to keratin intermediate filament aggregates. does not involve amyloid P component because it occurred when binding of the latter protein was inhibited by EDTA buffer. Moreover, purified vitronectin also bound to keratin intermediate filament aggregates in immunofluorescence studies. Vitronectin binding to keratin intermediate filaments may play a role both in limiting complement-mediated tissue damage (because keratin bodies may activate complement) and in promoting removal of keratin bodies by fibroblasts and/or macrophages.

Blotting, Western↗
PubMed1989

Immunohistochemical demonstration of age-related deposition of vitronectin (S-protein of complement) and terminal complement complex on dermal elastic fibers.

Immunoreactivity of vitronectin was investigated in 100 skin specimens from different body regions in 87 individuals of different ages using monoclonal and polyclonal anti-vitronectin antibodies in an avidin-biotin-peroxidase complex technique. Vitronectin immunoreactivity was found in conjunction with dermal elastic fibers in all subjects older than 13 years. No vitronectin immunostaining was detected in subjects younger than six years, suggesting deposition of vitronectin during late childhood or early adolescence. Using an immunogold staining procedure, vitronectin immunoreactivity was ultrastructurally localized to the periphery of elastic fibers. The blood level of vitronectin in 20 healthy newborns was 67% of the adult level, suggesting active biosynthesis already in the fetus. To investigate whether vitronectin is deposited as part of the SC5b-9 complex or as uncomplexed protein, the immunoreactivity of vitronectin was compared with that of C9, using monoclonal and polyclonal antibodies against the C9 neoantigen. Distinct C9 neoantigen immunoreactivity was demonstrated in association with dermal elastic fibers in human skin in adults but only in subjects older than 30 years. The intensity of C9 neoantigen immunoreactivity appeared to increase with age and was found to be stronger in sun-exposed skin than in sun-protected skin. These findings indicate that uncomplexed vitronectin is deposited during childhood or early adolescence and that terminal complement complexes (C5b-9 and/or SC5b-9) are deposited on elastic fibers later on in life. Hypothetically, the tissue form of vitronectin may be involved in the prevention of tissue damage in proximity to local complement activation. In addition, it may be physiologically important as substratum for cells, stimulating cell migration and anchorage.

Adolescent↗
PubMed1989

Vitronectin colocalizes with Ig deposits and C9 neoantigen in discoid lupus erythematosus and dermatitis herpetiformis, but not in bullous pemphigoid.

C9 neoantigen immunoreactivity has been found to colocalize with C3 immunoreactivity at the dermal-epidermal junction zone (DEZ) in skin specimens from patients with bullous pemphigoid, lupus erythematosus and dermatitis herpetiformis. The present study was designed to elucidate whether the C9 neoantigen immunoreactivity represents deposition of membrane attack complexes or non-lytic SC5b-9 complexes. Skin specimens from 11 patients with pemphigoid, five patients with discoid lupus erythematosus and from nine patients with dermatitis herpetiformis were studied with immunofluorescence using both monoclonal and polyclonal antibodies against C9 neoantigen and against vitronectin (S-protein), an inhibitor to the membrane attack complex of complement. Specimens from the pemphigoid patients demonstrated C9 neoantigen reactivity along the DEZ without detectable colocalized vitronectin. This suggests deposition of membrane attack complexes in the pemphigoid lesions. Immunoreactivity of both C9 neoantigen and vitronectin was detected in the DEZ in specimens of discoid lupus erythematosus and in the tips of dermal papillae in specimens of dermatitis herpetiformis. The combined presence of C9 neoantigen- and vitronectin immunoreactivity may indicate deposition of C9 as part of the non-lytic SC5b-9 complex. The finding reported here of differential deposition of vitronectin and C9 in different diseases indicates that the presence of C9 neoantigen immunoreactivity in tissue per se does not represent the deposition of membrane attack complexes, but that it may also be C9 deposited as part of the nonlytic SC5b-9 complex.

Autoantigens↗
PubMed1988

Immunohistochemical studies on vitronectin in elastic tissue disorders, cutaneous amyloidosis, lichen ruber planus and porphyria.

Vitronectin, identical with serum-spreading factor and S-protein of complement, is a glycoprotein present in both plasma and tissue. It stimulates cell adhesion and spreading and affects the complement and coagulation pathways. Vitronectin immunoreactivity was recently found in conjunction with dermal and renal elastic fibres, in renal amyloid deposits in cases of AL- and AA-amyloidosis, and in sclerotic glomerular lesions. Skin specimens from lesions of patients with selected skin diseases were investigated with an avidin-biotin peroxidase technique using both monoclonal and polyclonal anti-vitronectin antibodies and an alkaline phosphatase anti-alkaline phosphatase technique using monoclonal anti-vitronectin antibodies. Vitronectin immunoreactivity was found in association with the abnormal elastic tissue in solar elastosis and pseudoxanthoma elasticum. It was also found in conjunction with dermal amyloid deposits in primary localized cutaneous amyloidosis and in Civatte bodies in cases of lichen ruber planus. In cases of erythropoietic protoporphyria and porphyria cutanea tarda, hyaline perivascular deposits also demonstrated positive vitronectin immunoreactivity. The presence of vitronectin immunoreactivity not only in normal and degenerated elastic fibres but also in various pathological tissue deposits suggests that vitronectin occurs both in elastic fibres and in different types of abnormal protein deposits.

Amyloidosis↗
PubMed1987

Immunohistochemical demonstration of vitronectin in association with elastin and amyloid deposits in human kidney.

The multifunctional glycoprotein vitronectin, also called serum spreading factor and S-protein of complement, is a potent inducer of cell adhesion and spreading in vitro, and also has a regulatory function in the complement and coagulation pathways. It is present both in plasma and tissue. Recently, vitronectin immunoreactivity was demonstrated in the elastic fibres of normal human skin. Normal and amyloid kidney tissue was investigated for vitronectin immunoreactivity using polyclonal and monoclonal antibodies in an avidin-biotin-peroxidase complex technique and in an alkaline phosphatase anti-alkaline phosphatase complex technique. Vitronectin was found in the elastic layers of normal vessel walls, and in glomerular sclerotic lesions in cases of benign nephrosclerosis, but not in normal glomeruli. Strong specific vitronectin immunoreactivity was found in the amyloid deposits in kidneys from cases with amyloid A type amyloidosis, and in cases with amyloid light chain type amyloidosis. Structures immunostainable with anti-amyloid A antiserum were invariably immunostainable with anti-vitronectin. An antiserum against serum amyloid P component stained the same structures as did the anti-vitronectin antibodies, and in addition stained normal glomerular basement membranes. In conclusion, vitronectin immunoreactivity was demonstrated in elastic tissue, in amyloid deposits and in sclerotic lesions in human kidney.

Amyloid↗
PubMed1986

Localization of vitronectin (S-protein of complement) in normal human skin.

Vitronectin, now known to be identical to serum spreading factor and to S-protein of complement, is a multifunctional glycoprotein involved in the adhesion and spreading of cells and in the complement and coagulation pathways. The distribution of vitronectin in normal human skin was investigated with immunofluorescence using polyclonal antibodies, and with an avidin-biotin peroxidase complex technique, using polyclonal as well as monoclonal antibodies. Vitronectin immunreactivity was found to be localized on the elastic fibres in the dermis. Both the thin fibres in the papillary dermis and the thicker elastic fibres in the reticular dermis were stained. No crossreactivity was found between vitronectin and serum amyloid P component, known to bind to elastic fibres. The two proteins were immunohistochemically localized to the same structures in the skin. The distribution of vitronectin in the dermal tissue established in this study provides a basis for further studies of the function and behaviour of vitronectin in health and disease.

Fluorescent Antibody Technique↗