Dermatologist, Board Certified Mohs Surgeon
8 years of experience

Accepting new patients
Pennsylvania Dermatology Partners
2913 Windmill Rd
Ste 7
Reading, PA 19608
(610) 288-2908
Locations and availability (3)

Education ?

Medical School Score Rankings
Temple University Physicians (2002)
  • Currently 3 of 4 apples
Top 50%
Fellowship
Dermatologic Surgi Center (2008) *
MOHS-Micrographic Surgery
* This information was reported to Vitals by the doctor or doctor's office.

Awards & Distinctions ?

Associations
American Board of Dermatology
Diplomat, Board Certified
American Society for Dermatologic Surgery
Member
American College of Mohs Surgery
Fellow
American Academy of Dermatology
Member
American Society for Laser Medicine and Surgery
Member
Philadelphia Dermatologic Society
Member
Pennsylvania Medical Society
Member
Berks County Medical Society
Member

Affiliations ?

Dr. Shurman is affiliated with 1 hospitals.

Hospital Affilations

  • Reading Hospital & Medical Center
    601 Spruce St, West Reading, PA 19611
  • Publications & Research

    Dr. Shurman has contributed to 3 publications.
    Title Malignant Proliferating Pilar Tumors Arising in Kid Syndrome: a Report of Two Patients.
    Date October 2007
    Journal American Journal of Medical Genetics. Part A
    Excerpt

    We report on two young adults with KID syndrome and follicular hyperkeratosis, hidradenitis suppurativa of the groin, progressive development of proliferative pilar cysts and dissecting cellulitis of the scalp, who developed metastatic malignant pilar tumors. Based on our findings, we believe that cancer surveillance in patients with KID syndrome should include screening for pilar tumors and their early removal to avoid development of malignant proliferating pilar tumors with poor prognosis.

    Title In Vivo and in Vitro Expression of Connexins in the Human Corneal Epithelium.
    Date July 2005
    Journal Investigative Ophthalmology & Visual Science
    Excerpt

    PURPOSE: This study is designed to provide a comprehensive expression profile of connexins in the human corneal epithelium (in vivo) and in cultured primary corneal epithelial cells (PCECs) (in vitro). It also evaluates the pathologic effects of a pathogenic missense mutation in Cx26, which causes keratitis-ichthyosis-deafness syndrome (KIDS), a rare genetic disorder with corneal involvement. METHODS: RT-PCR analysis, immunohistochemistry, and fluorescent dye transfer assays were used to determine the expression pattern and gap junction intercellular communication in PCECs and human cornea. Differentiation-dependent differences in connexin expression of PCECs after a calcium switch were verified by real-time RT-PCR. The common KIDS mutation Cx26(D50N) was studied by determining transient expression in PCECs. RESULTS: In vivo immunostaining revealed widespread and overlapping expression of Cx43 and -30 in the basal and suprabasal layers. Cx26 staining was limited to the lower suprabasal cells, whereas Cx31.1 localized to the apical surface of basal cells in the central cornea and to the lower and middle suprabasal cells in the limbal region. Immunostaining for nine other connexins, including Cx50, was negative. In PCEC, nine connexin genes were detectable by RT-PCR, however, only Cx26, -30, and -43 formed visible gap junction plaques. High-Ca(2+) culture conditions were accompanied by a 1.6- to 2.2-fold upregulation of expression of Cx26, -30, and -43 and a significant increase in gap-junction-mediated dye transfer. Transient expression of mutant Cx26(D50N) in PCECs resulted in cytoplasmic accumulation and lack of gap junction plaque formation and was not altered by coexpression of wild-type (wt)Cx26 or -30. CONCLUSIONS: Gap junction communication in the human corneal epithelium is mediated by Cx26, -30, -31.1, and -43. Poorly differentiated PCECs are uncoupled, and Ca(2+) induced differentiation is associated with an upregulation of connexin expression and intercellular communication. The transfection experiments suggest that KIDS Cx26(D50N) impairs intracellular formation and transport of connexons formed by Cx26 and -30, consistent with a dominant negative effect.

    Title Mutations in Galnt3, Encoding a Protein Involved in O-linked Glycosylation, Cause Familial Tumoral Calcinosis.
    Date June 2004
    Journal Nature Genetics
    Excerpt

    Familial tumoral calcinosis (FTC; OMIM 211900) is a severe autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Using linkage analysis, we mapped the gene underlying FTC to 2q24-q31. This region includes the gene GALNT3, which encodes a glycosyltransferase responsible for initiating mucin-type O-glycosylation. Sequence analysis of GALNT3 identified biallelic deleterious mutations in all individuals with FTC, suggesting that defective post-translational modification underlies the disease.

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