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1.
Dermatol Surg ; 24(6): 633-6, 1998 Jun.
Article in English | MEDLINE | ID: mdl-9648570

ABSTRACT

BACKGROUND: Carbon dioxide laser resurfacing has gained popularity as a relatively safe and effective method of facial rejuvenation. Original reports describe mostly reversible side effects and a low incidence of scarring. Only very recently have reports of delayed hypopigmentation surfaced. This effect is not visible until several months after resurfacing, and most likely represents a permanent change. OBJECTIVE: To provide an additional clinical description of the complication of delayed hypopigmentation along with the first published histologic correlation. METHODS: Clinical records along with a preprocedure and 7-month postprocedure full-thickness skin biopsy were used for this report. RESULTS: This patient experienced a striking leukoderma 6 months after a full facial carbon dioxide laser resurfacing procedure done for widespread actinic keratoses. There was a zone of dermal fibrosis extending approximately 0.4 mm on the postprocedure biopsy. Comparison of the preprocedure and postprocedure biopsies revealed no difference in the number of melanocytes by MART-1 immunohistochemical staining, but there was a significant decrease in epidermal melanin as determined by Fontana-Mason staining. CONCLUSION: This patient experienced a profound expression of an increasingly recognized and reported complication of carbon dioxide laser resurfacing. Histologic correlation is similar to the results previously reported after phenol chemical peels, demonstrating a normal number of melanocytes but a decrease in epidermal melanin.


Subject(s)
Hypopigmentation/etiology , Hypopigmentation/pathology , Keratosis/surgery , Laser Therapy/adverse effects , Carbon Dioxide , Female , Humans , Laser Therapy/methods , Middle Aged
2.
Am Fam Physician ; 57(8): 1860-4, 1998 Apr 15.
Article in English | MEDLINE | ID: mdl-9575324

ABSTRACT

Basal cell carcinoma is the most common skin malignancy. While this lesion most often occurs in sun-exposed areas of the skin, it can also develop in sites that are not usually exposed to sunlight or artificial ultraviolet radiation, such as the breast, palm or groin. A periodic complete examination of the skin should be performed to ensure that atypical presentations of basal cell carcinoma are not overlooked or misdiagnosed. Treatment options include curettage and desiccation, cryosurgery, surgical excision, radiotherapy and Mohs micrographic surgery.


Subject(s)
Axilla , Carcinoma, Basal Cell , Skin Neoplasms , Aged , Carcinoma, Basal Cell/diagnosis , Carcinoma, Basal Cell/etiology , Carcinoma, Basal Cell/therapy , Diagnosis, Differential , Humans , Male , Skin Neoplasms/diagnosis , Skin Neoplasms/etiology , Skin Neoplasms/therapy
3.
Dermatol Surg ; 24(2): 233-40, 1998 Feb.
Article in English | MEDLINE | ID: mdl-9491118

ABSTRACT

BACKGROUND: Electrosurgery is frequently employed in the treatment of skin cancer and other dermatologic conditions in the elderly. Implantable cardioverter-defibrillators (ICDs) and pacemakers are most commonly seen in this older population. Potentially hazardous electrosurgical interference exists with the function of ICDs and pacemakers in this setting. OBJECTIVE: Our goal is to review the potential hazards of electrosurgery in patients with ICDs and pacemakers and to suggest a perioperative management plan. METHODS: Review of the medical literature on electrosurgical interference with ICDs and pacemakers was accomplished in addition to a case report of ventricular tachycardia during Mohs surgery on a patient with an ICD. RESULTS: Multiple case reports and reviews from the nonder-matologic literature demonstrate that a real hazard exists. CONCLUSION: Knowledge of the potential electrosurgical interference with ICDs and pacemakers is required to perform these procedures safely. A perioperative management plan is suggested.


Subject(s)
Defibrillators, Implantable , Dermatologic Surgical Procedures , Electrosurgery , Pacemaker, Artificial , Aged , Aged, 80 and over , Carcinoma, Basal Cell/surgery , Carcinoma, Squamous Cell/surgery , Contraindications , Electrosurgery/adverse effects , Facial Neoplasms/surgery , Humans , Male , Mohs Surgery , Preoperative Care , Skin Neoplasms/surgery
4.
Lasers Surg Med ; 22(1): 10-3, 1998.
Article in English | MEDLINE | ID: mdl-9443144

ABSTRACT

BACKGROUND AND OBJECTIVE: We report two cases of hemangiomas in twins born at a gestational age of 30 weeks who were treated with a flashlamp-pumped pulsed dye laser (FPDL) at 40 days postpartem. These were the youngest patients to our knowledge to be treated with FPDL. STUDY DESIGN/PATIENTS AND METHODS: Twin Caucasian females were born 10 weeks preterm. Twin A soon developed a 1 cm blanching erythematous patch with telangiectasia on a slightly bulbous nasal tip. Twin B developed a 6 mm erythematous papule on her forehead, a 12 x 10 cm erythematous plaque on her left shoulder, and two plaques measuring 2.5 x 2.0 cm and 1.5 x 1.0 cm on her right hip. The twins received seven monthly laser treatments. RESULTS: Several of the hemangiomas showed remarkable regression, including the lesions which became ulcerated and healed on Twin B's left shoulder and right hip. No general or topical anesthesia was used and the twins tolerated the procedure well. No significant adverse effects were encountered. The maximum single treatment dose was 7 mm spot size, 5.0 J/cm2 and 186 pulses for twin B and 6.25 J/cm2 and 16 pulses for twin A. CONCLUSION: To our knowledge, our patients are the youngest reported to be treated with FPDL at age 30 days preterm. Some of their hemangiomas responded, and no significant adverse effects were encountered. More prospective trials are needed to determine whether early treatment with FPDL accelerates regression of hemangiomas or results in a better cosmetic outcome than expectant treatment.


Subject(s)
Diseases in Twins , Hemangioma/surgery , Infant, Premature , Laser Therapy/methods , Skin Neoplasms/surgery , Female , Follow-Up Studies , Gestational Age , Humans , Infant, Newborn
6.
J Am Acad Dermatol ; 34(3): 465-9, 1996 Mar.
Article in English | MEDLINE | ID: mdl-8609261

ABSTRACT

BACKGROUND: Hidradenitis suppurativa is a disabling disease. Although medical management can at times control the disease, the treatment of choice is surgical excision. Surgical defects have been managed by second-intention healing, simple surgical closure, or complex surgical repairs. OBJECTIVE: Our purpose was to determine the benefit of carbon dioxide laser excision with healing by second intention to treat lesions of hidradenitis suppurativa. METHODS: We treated seven patients who had axillary and inguinoperineal hidradenitis suppurativa with carbon dioxide laser excision followed by second-intention healing. A total of 12 procedures were performed (five bilateral and two unilateral). Follow-up periods were 10 to 27 months. RESULTS: After a healing time of 4 to 8 weeks, scars were flat and linear. Only one recurrence of hidradenitis suppurativa has been observed; this occurred along the margin of the surgical scar in a previously treated area. Some patients, however, had continued disease activity in untreated areas. All subjects were satisfied with the results of the procedure, and complications were minimal. CONCLUSION: Carbon dioxide laser excision with second-intention healing is safe and effective for hidradenitis suppurativa.


Subject(s)
Hidradenitis Suppurativa/surgery , Laser Therapy , Adult , Axilla/surgery , Carbon Dioxide , Cicatrix/pathology , Cicatrix/prevention & control , Female , Follow-Up Studies , Groin/surgery , Humans , Laser Therapy/adverse effects , Laser Therapy/methods , Middle Aged , Patient Satisfaction , Perineum/surgery , Recurrence , Wound Healing
7.
J Biol Chem ; 269(49): 31259-66, 1994 Dec 09.
Article in English | MEDLINE | ID: mdl-7983070

ABSTRACT

The subcellular distribution and targeting of the non-lysosomal aspartic proteinase cathepsin E have been studied using mouse L cells and monkey Cos 1 cells that were transfected with cDNA encoding cathepsin E. The cathepsin E was retained in L cells for at least 20 h without significant degradation and its single N-linked oligosaccharide remained sensitive to endo-beta-N-acetyl-glucosaminidase H. When cathepsin E was overexpressed by transient transfection in Cos 1 cells, it was very slowly secreted into the media. The intracellular form of the enzyme contained a high mannose oligosaccharide which was processed to a complex type species upon secretion. In double label immunofluorescence studies, cathepsin E co-localized with cathepsin D-myc-KDEL, an endoplasmic reticulum (ER) marker. Subcellular fractionation on a Percoll density gradient showed that the cathepsin E co-migrated with membranous vesicles that were distinct from dense lysosomes. Only a trace amount of the enzyme was recovered in the soluble fraction. These findings indicate that in L cells and Cos 1 cells, the intracellular location of cathepsin E is the endoplasmic reticulum. To identify the protein sequences required for ER retention, we made chimeric proteins between cathepsin E and pepsinogen, an aspartic proteinase that is rapidly secreted by Cos 1 cells. We found that amino acids 1-48 of cathepsin E are important for its retention in the ER. Within this region, Cys7, which is involved in covalent dimer formation, plays a significant role in the retention.


Subject(s)
Cathepsins/metabolism , Subcellular Fractions/enzymology , Alternative Splicing , Amino Acid Sequence , Animals , Antibodies , Base Sequence , Cathepsin E , Cathepsins/genetics , Cathepsins/immunology , Cell Line , Cross-Linking Reagents , Endoplasmic Reticulum/enzymology , Fluorescent Antibody Technique , Haplorhini , L Cells/enzymology , Mice , Molecular Sequence Data , Oligodeoxyribonucleotides , Pepstatins/metabolism , Protein Binding , Rats , Recombinant Fusion Proteins/metabolism , Sepharose/metabolism
8.
Arch Dermatol ; 130(8): 1055, 1058, 1994 Aug.
Article in English | MEDLINE | ID: mdl-8053707
10.
Proc Natl Acad Sci U S A ; 88(12): 5192-6, 1991 Jun 15.
Article in English | MEDLINE | ID: mdl-1647027

ABSTRACT

The protein responsible for both nucleotide pyrophosphatase (EC 3.6.1.9) and alkaline phosphodiesterase I (EC 3.1.4.1) activities was purified from MOPC 315 plasmacytoma cells. A single SDS/PAGE-purified 115-kDa protein band was used to produce a rabbit polyclonal antiserum. This antibody preparation precipitated alkaline phosphodiesterase I activity, indicating that the SDS/PAGE-purified protein was nucleotide pyrophosphatase/alkaline phosphodiesterase I. When used for Western blot analysis, the antiserum detected a 115-kDa protein as well as a 220-kDa protein band. Multiple overlapping cDNA clones were isolated from a cDNA expression library screened with this anti-nucleotide pyrophosphatase/alkaline phosphodiesterase I antiserum. Sequence analysis indicated that the isolated cDNA clones encoded PC-1, a murine plasma cell differentiation antigen. To confirm the suspected enzymatic identity of PC-1, a recombinant PC-1 fusion protein was expressed in bacteria, purified, and used to produce another rabbit polyclonal antiserum. This antiserum likewise immunoprecipitated alkaline phosphodiesterase I activity and recognized the 115-kDa and 220-kDa proteins in Western blot analyses of cell extracts. Furthermore, expression of nucleotide pyrophosphatase/alkaline phosphodiesterase I corresponded directly with mRNA and protein levels of PC-1 in cells known to express different levels of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity. Finally, steroid induction of enzymatic activity was mirrored by levels of PC-1 mRNA and protein expression. Together, these data indicate that the plasma cell differentiation antigen PC-1 is a membrane-bound enzyme, nucleotide pyrophosphatase/alkaline phosphodiesterase I.


Subject(s)
Antigens, Differentiation, B-Lymphocyte/metabolism , Phosphoric Diester Hydrolases/metabolism , Pyrophosphatases/metabolism , Animals , Blotting, Northern , Blotting, Western , DNA/genetics , Electrophoresis, Polyacrylamide Gel , Mice , Phosphodiesterase I , Precipitin Tests , RNA, Messenger/genetics
11.
Arch Biochem Biophys ; 279(2): 395-401, 1990 Jun.
Article in English | MEDLINE | ID: mdl-2350186

ABSTRACT

The glycosylation and processing of the asparagine-linked oligosaccharides at individual glycosylation sites on the mu-chain of murine immunoglobulin M were investigated using variant cell lines that synthesize and secrete IgM heavy chains with known peptide deletions. Normal murine IgM has five N-linked oligosaccharides in the constant region of each heavy or mu-chain. Each mu-chain has four complex-type oligosaccharides as well as a single high mannose-type oligosaccharide near the carboxyl terminus of the molecule. The peptide deletion of the C mu 1 constant region domain in the heavy chains synthesized by one variant cell line did not prevent subsequent glycosylation at more distal glycosylation sites. In fact, the presence of this deletion resulted in more complete glycosylation at the C-terminal glycosylation site. Evaluation of glycopeptides containing individual glycosylation sites by Concanavalin A-Sepharose indicated that this deletion had no significant effect on the processing of structures from high mannose-type to complex-type oligosaccharide chains. In contrast, a deletion of the C-terminal peptide region of the heavy chain of IgM synthesized by a second variant cell line resulted in intracellular processing to more highly branched oligosaccharide structures at several of the glycosylation sites not involved in the deletion.


Subject(s)
Immunoglobulin M/metabolism , Animals , Chromatography, Gel , Glycopeptides/analysis , Glycosylation , Hybridomas , Immunoglobulin M/genetics , Mice , Mutation , Protein Processing, Post-Translational , Structure-Activity Relationship
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