Impact of internet-based cancer survivorship care plans on health care and lifestyle behaviors.

BACKGROUND: Survivorship care plans (SCP) are currently recommended by the Institute of Medicine, and will soon be required for accreditation by the American College of Surgeons Commission on Cancer. To the best of the authors' knowledge, the impact of SCPs on cancer survivors has not been previously reported. METHODS: In 2007, the authors created an Internet tool for the creation of SCPs that provides customized guidelines for survivorship care. Users are sent a voluntary follow-up survey 1 month after initial use. RESULTS: From May 2010 through January 2013, 8690 cancer survivors used the SCP tool. The most common diagnoses were breast (45%), hematologic (12%), and gastrointestinal (11%) cancers; the median age of the survivors was 51 years. Of these, 875 (10%) respondents provided information for future electronic contact and 298 responded to a 1-month follow-up survey. They reported that the information provided was "good" to "excellent" in 93% of cases, and new in 65% of cases. With regard to the emotional impact of the SCP, 62% of responding survivors believed that it provided "just enough" information, 72% felt "more informed," and 94% believed they would recommend it to others. The majority of respondents (63%) thought that the SCP changed their health care participation, and 80% shared/planned to share it with their health care team. Of those survivors who had done so, 80% reported that it improved communication with their health care providers. Greater than one-half of survey users (54%) reported that they had made or planned to make a lifestyle change in response to the SCP, most commonly dietary modification and increased exercise. CONCLUSIONS: Survivorship care plans are useful vehicles with which to promote lifestyle and behavioral changes, and to assist survivors with communication with health care providers. These findings support recommendations from the Institute of Medicine and the American College of Surgeons Commission on Cancer.

Cosmetic outcomes and complications reported by patients having undergone breast-conserving treatment.

PURPOSE: Over the past 30 years, much work in treatment of breast cancer has contributed to improvement of cosmetic and functional outcomes. The goal of breast-conservation treatment (BCT) is avoidance of mastectomy through use of lumpectomy and adjuvant radiation. Modern data demonstrate "excellent" or "good" cosmesis in >90% of patients treated with BCT. METHODS AND MATERIALS: Patient-reported data were gathered via a convenience sample frame from breast cancer survivors using a publically available, free, Internet-based tool for creation of survivorship care plans. During use of the tool, breast cancer survivors are queried as to the cosmetic appearance of the treated breast, as well as perceived late effects. All data have been maintained anonymously with internal review board approval. RESULTS: Three hundred fifty-four breast cancer survivors having undergone BCT and voluntarily using this tool were queried with regard to breast cosmesis and perceived late effects. Median diagnosis age was 48 years, and median current age 52 years. "Excellent" cosmesis was reported by 27% (n = 88), "Good" by 44% (n = 144), "Fair" by 24% (n = 81), and "Poor" by 5% (n = 18). Of the queries posted to survivors after BCT, late effects most commonly reported were cognitive changes (62%); sexual concerns (52%); changes in texture and color of irradiated skin (48%); chronic pain, numbness, or tingling (35%); and loss of flexibility in the irradiated area (30%). Survivors also described osteopenia/osteoporosis (35%), cardiopulmonary problems (12%), and lymphedema (19%). CONCLUSIONS: This anonymous tool uses a convenience sample frame to gather patient reported assessments of cosmesis and complications after breast cancer. Among the BCT population, cosmetic assessment by survivors appears less likely to be "excellent" or "good" than would be expected, with 30% of BCT survivors reporting "fair" or "poor" cosmesis. Patient reported incidence of chronic pain, as well as cognitive and sexual changes, also appears higher than expected.

Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates.

Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens and non-collagenous molecules into large cable-like fibrils, yet how the fibril interacts with cells and other binding partners remains poorly understood. To help reveal insights into the collagen structure-function relationship, a data base was assembled including hundreds of type I collagen ligand binding sites and mutations on a two-dimensional model of the fibril. Visual examination of the distribution of functional sites, and statistical analysis of mutation distributions on the fibril suggest it is organized into two domains. The "cell interaction domain" is proposed to regulate dynamic aspects of collagen biology, including integrin-mediated cell interactions and fibril remodeling. The "matrix interaction domain" may assume a structural role, mediating collagen cross-linking, proteoglycan interactions, and tissue mineralization. Molecular modeling was used to superimpose the positions of functional sites and mutations from the two-dimensional fibril map onto a three-dimensional x-ray diffraction structure of the collagen microfibril in situ, indicating the existence of domains in the native fibril. Sequence searches revealed that major fibril domain elements are conserved in type I collagens through evolution and in the type II/XI collagen fibril predominant in cartilage. Moreover, the fibril domain model provides potential insights into the genotype-phenotype relationship for several classes of human connective tissue diseases, mechanisms of integrin clustering by fibrils, the polarity of fibril assembly, heterotypic fibril function, and connective tissue pathology in diabetes and aging.

Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion.

Non-enzymatic glycation of type I collagen occurs in aging and diabetes, and may affect collagen solubility, charge, polymerization, and intermolecular interactions. Proteoglycans(1) (PGs) bind type I collagen and are proposed to regulate fibril assembly, function, and cell-collagen interactions. Moreover, on the collagen fibril a keratan sulfate (KS) PG binding region overlaps with preferred collagen glycation sites. Thus, we examined the effect of collagen modified by simple glycation on PG-collagen interactions. By affinity coelectrophoresis (ACE), we found reduced affinities of heparin and KSPGs for glycated but not normal collagen, whereas the dermatan sulfate (DS)PGs decorin and biglycan bound similarly to both, and that the affinity of heparin for normal collagen decreased with increasing pH. Circular dichroism (CD) spectroscopy revealed normal and glycated collagens to assume triple helical conformations, but heparin addition caused precipitation and decreased triple helical content-effects that were more marked with glycated collagen. A spectrophotometric assay revealed slower polymerization of glycated collagen. However, ultrastructural analyses indicated that fibrils assembled from normal and glycated collagen exhibited normal periodicity, and had similar structures and comparable diameter distributions. B-cells expressing the cell surface heparan sulfate PG syndecan-1 adhered well to normal but not glycated collagen, and endothelial cell migration was delayed on glycated collagen. We speculate that glycation diminishes the electrostatic interactions between type I collagen and PGs, and may interfere with core protein-collagen associations for KSPGs but not DSPGs. Therefore in vivo, collagen glycation may weaken PG-collagen interactions, thereby disrupting matrix integrity and cell-collagen interactions, adhesion, and migration.

Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen.

Type I collagen is the most abundant protein in humans, and it helps to maintain the integrity of many tissues via its interactions with cell surfaces, other extracellular matrix molecules, and growth and differentiation factors. Nearly 50 molecules have been found to interact with type I collagen, and for about half of them, binding sites on this collagen have been elucidated. In addition, over 300 mutations in type I collagen associated with human connective tissue disorders have been described. However, the spatial relationships between the known ligand-binding sites and mutation positions have not been examined. To this end, here we have created a map of type I collagen that includes all of its ligand-binding sites and mutations. The map reveals the existence of several hot spots for ligand interactions on type I collagen and that most of the binding sites locate to its C-terminal half. Moreover, on the collagen fibril some potentially relevant relationships between binding sites were observed including the following: fibronectin- and certain integrin-binding regions are near neighbors, which may mechanistically relate to fibronectin-dependent cell-collagen attachment; proteoglycan binding may potentially impact upon collagen fibrillogenesis, cell-collagen attachment, and collagen glycation seen in diabetes and aging; and mutations associated with osteogenesis imperfecta and other disorders show apparently nonrandom distribution patterns within both the monomer and fibril, implying that mutation positions correlate with disease phenotype. These and other observations presented here may provide novel insights into evaluating type I collagen functions and the relationships between its binding partners and mutations.